Primase

Last updated
Toprim domain
Identifiers
SymbolToprim
Pfam PF01751
Pfam clan Toprim-like
InterPro IPR006171
SCOP2 2fcj / SCOPe / SUPFAM
Available protein structures:
Pfam   structures / ECOD  
PDB RCSB PDB; PDBe; PDBj
PDBsum structure summary
Toprim catalytic core
Identifiers
SymbolToprim_N
Pfam PF08275
InterPro IPR013264
SCOP2 1dd9 / SCOPe / SUPFAM
Available protein structures:
Pfam   structures / ECOD  
PDB RCSB PDB; PDBe; PDBj
PDBsum structure summary
AEP DNA primase, small subunit
Identifiers
SymbolDNA_primase_S
Pfam PF01896
Pfam clan AEP
InterPro IPR002755
SCOP2 1g71 / SCOPe / SUPFAM
Available protein structures:
Pfam   structures / ECOD  
PDB RCSB PDB; PDBe; PDBj
PDBsum structure summary
AEP DNA primase, large subunit
Identifiers
SymbolDNA_primase_lrg
Pfam PF04104
Pfam clan CL0242
InterPro IPR007238
SCOP2 1zt2 / SCOPe / SUPFAM
Available protein structures:
Pfam   structures / ECOD  
PDB RCSB PDB; PDBe; PDBj
PDBsum structure summary

DNA primase is an enzyme involved in the replication of DNA and is a type of RNA polymerase. Primase catalyzes the synthesis of a short RNA (or DNA in some living organisms [1] ) segment called a primer complementary to a ssDNA (single-stranded DNA) template. After this elongation, the RNA piece is removed by a 5' to 3' exonuclease and refilled with DNA.

Contents

Function

Asymmetry in the synthesis of leading and lagging strands, with role of DNA primase shown Asymmetry in the synthesis of leading and lagging strands.svg
Asymmetry in the synthesis of leading and lagging strands, with role of DNA primase shown
Steps in DNA synthesis, with role of DNA primase shown Steps in DNA synthesis.svg
Steps in DNA synthesis, with role of DNA primase shown

In bacteria, primase binds to the DNA helicase forming a complex called the primosome. Primase is activated by the helicase where it then synthesizes a short RNA primer approximately 11 ±1 nucleotides long, to which new nucleotides can be added by DNA polymerase. Archaeal and eukaryote primases are heterodimeric proteins with one large regulatory and one minuscule catalytic subunit. [2]

The RNA segments are first synthesized by primase and then elongated by DNA polymerase. [3] Then the DNA polymerase forms a protein complex with two primase subunits to form the alpha DNA Polymerase primase complex. Primase is one of the most error prone and slow polymerases. [3] Primases in organisms such as E. coli synthesize around 2000 to 3000 primers at the rate of one primer per second. [4] Primase also acts as a halting mechanism to prevent the leading strand from outpacing the lagging strand by halting the progression of the replication fork. [5] The rate determining step in primase is when the first phosphodiester bond is formed between two molecules of RNA. [3]

The replication mechanisms differ between different bacteria and viruses where the primase covalently link to helicase in viruses such as the T7 bacteriophage. [5] In viruses such as the herpes simplex virus (HSV-1), primase can form complexes with helicase. [6] The primase-helicase complex is used to unwind dsDNA (double-stranded) and synthesizes the lagging strand using RNA primers [6] The majority of primers synthesized by primase are two to three nucleotides long. [6]

Types

There are two main types of primase: DnaG found in most bacteria, and the AEP (Archaeo-Eukaryote Primase) superfamily found in archaean and eukaryotic primases. While bacterial primases (DnaG-type) are composed of a single protein unit (a monomer) and synthesize RNA primers, AEP primases are usually composed of two different primase units (a heterodimer) and synthesize two-part primers with both RNA and DNA components. [7] While functionally similar, the two primase superfamilies evolved independently of each other.

DnaG

The crystal structure of primase in E. coli with a core containing the DnaG protein was determined in the year 2000. [4] The DnaG and primase complex is cashew shaped and contains three subdomains. [4] The central subdomain forms a toprim fold which is made of a mixture five beta sheets and six alpha helices. [4] [8] The toprim fold is used for binding regulators and metals. The primase uses a phosphotransfer domain for the transfer coordination of metals, which makes it distinct from other polymerases. [4] The side subunits contain a NH2 and COOH terminal made of alpha helixes and beta sheets. [4] The NH2 terminal interacts with a zinc binding domain and COOH-terminal region which interacts with DnaB-ID. [4]

The Toprim fold is also found in topoisomerase and mitochrondrial Twinkle primase/helicase. [8] Some DnaG-like (bacteria-like; InterPro :  IPR020607 ) primases have been found in archaeal genomes. [9]

AEP

Eukaryote and archaeal primases tend to be more similar to each other, in terms of structure and mechanism, than they are to bacterial primases. [10] [11] The archaea-eukaryotic primase (AEP) superfamily, which most eukaryal and archaeal primase catalytic subunits belong to, has recently been redefined as a primase-polymerase family in recognition of the many other roles played by enzymes in this family. [12] This classification also emphasizes the broad origins of AEP primases; the superfamily is now recognized as transitioning between RNA and DNA functions. [13]

Archaeal and eukaryote primases are heterodimeric proteins with one large regulatory (human PRIM2, p58) and one small catalytic subunit (human PRIM1, p48/p49). [2] The large subunit contains a N-terminal 4Fe–4S cluster, split out in some archaea as PriX/PriCT. [14] The large subunit is implicated in improving the activity and specificity of the small subunit. For example, removing the part corresponding to the large subunit in a fusion protein PolpTN2 results in a slower enzyme with reverse transcriptase activity. [13]

Multifunctional primases

Figure 1. Select multifunctional primases across three domains of life (eukaryota, archaea, and bacteria). The ability of a primase to perform a particular activity is indicated by a check mark. Adapted from. Multifunctional primases figure.jpg
Figure 1. Select multifunctional primases across three domains of life (eukaryota, archaea, and bacteria). The ability of a primase to perform a particular activity is indicated by a check mark. Adapted from.

The AEP family of primase-polymerases has diverse features beyond making only primers. In addition to priming DNA during replication, AEP enzymes may have additional functions in the DNA replication process, such as polymerization of DNA or RNA, terminal transfer, translesion synthesis (TLS), non-homologous end joining (NHEJ), [12] and possibly in restarting stalled replication forks. [15] Primases typically synthesize primers from ribonucleotides (NTPs); however, primases with polymerase capabilities also have an affinity for deoxyribonucleotides (dNTPs). [16] [11] Primases with terminal transferase functionality are capable of adding nucleotides to the 3’ end of a DNA strand independently of a template. Other enzymes involved in DNA replication, such as helicases, may also exhibit primase activity. [17]

In eukaryotes and archaea

Human PrimPol (ccdc111 [16] ) serves both primase and polymerase functions, like many archaeal primases; exhibits terminal transferase activity in the presence of manganese; and plays a significant role in translesion synthesis [18] and in restarting stalled replication forks. PrimPol is actively recruited to damaged sites through its interaction with RPA, an adapter protein that facilitates DNA replication and repair. [15] PrimPol has a zinc finger domain similar to that of some viral primases, which is essential for translesion synthesis and primase activity and may regulate primer length. [18] Unlike most primases, PrimPol is uniquely capable of starting DNA chains with dNTPs. [16]

PriS, the archaeal primase small subunit, has a role in translesion synthesis (TLS) and can bypass common DNA lesions. Most archaea lack the specialized polymerases that perform TLS in eukaryotes and bacteria. [19] PriS alone preferentially synthesizes strings of DNA; but in combination with PriL, the large subunit, RNA polymerase activity is increased. [20]

In Sulfolobus solfataricus, the primase heterodimer PriSL can act as a primase, polymerase, and terminal transferase. PriSL is thought to initiate primer synthesis with NTPs and then switch to dNTPs. The enzyme can polymerize RNA or DNA chains, with DNA products reaching as long as 7000 nucleotides (7 kb). It is suggested that this dual functionality may be a common feature of archaeal primases. [11]

In bacteria

AEP multifutional primases also appear in bacteria and phages that infect them. They can display novel domain organizations with domains that bring even more functions beyond polymerization. [14]

Bacterial LigD ( A0R3R7 ) is primarily involved in the NHEJ pathway. It has an AEP superfamily polymerase/primase domain, a 3'-phosphoesterase domain, and a ligase domain. It is also capable of primase, DNA and RNA polymerase, and terminal transferase activity. DNA polymerization activity can produce chains over 7000 nucleotides (7 kb) in length, while RNA polymerization produces chains up to 1 kb long. [21]

In viruses and plasmids

AEP enzymes are widespread, and can be found encoded in mobile genetic elements including virus/phages and plasmids. They either use them as a sole replication protein or in combination with other replication-associated proteins, such as helicases and, less frequently, DNA polymerases. [22] Whereas the presence of AEP in eukaryotic and archaeal viruses is expected in that they mirror their hosts, [22] bacterial viruses and plasmids also as frequently encode AEP-superfamily enzymes as they do DnaG-family primases. [14] A great diversity of AEP families has been uncovered in various bacterial plasmids by comparative genomics surveys. [14] Their evolutionary history is currently unknown, as these found in bacteria and bacteriophages appear too different from their archaeo-eukaryotic homologs for a recent horizontal gene transfer. [22]

MCM-like helicase in Bacillus cereus strain ATCC 14579 (BcMCM; Q81EV1 ) is an SF6 helicase fused with an AEP primase. The enzyme has both primase and polymerase functions in addition to helicase function. The gene coding for it is found in a prophage. [17] It bears homology to ORF904 of plasmid pRN1 from Sulfolobus islandicus, which has an AEP PrimPol domain. [23] Vaccinia virus D5 and HSV Primase are examples of AEP-helicase fusion as well. [12] [6]

PolpTN2 is an Archaeal primase found in the TN2 plasmid. A fusion of domains homologous to PriS and PriL, it exhibits both primase and DNA polymerase activity, as well as terminal transferase function. Unlike most primases, PolpTN2 forms primers composed exclusively of dNTPs. [13] Unexpectedly, when the PriL-like domain was truncated, PolpTN2 could also synthesize DNA on the RNA template, i.e., acted as an RNA-dependent DNA polymerase (reverse transcriptase). [13]

Even DnaG primases can have extra functions, if given the right domains. The T7 phage gp4 is a DnaG primase-helicase fusion, and performs both functions in replication. [5]

Related Research Articles

<span class="mw-page-title-main">DNA replication</span> Biological process

In molecular biology, DNA replication is the biological process of producing two identical replicas of DNA from one original DNA molecule. DNA replication occurs in all living organisms acting as the most essential part of biological inheritance. This is essential for cell division during growth and repair of damaged tissues, while it also ensures that each of the new cells receives its own copy of the DNA. The cell possesses the distinctive property of division, which makes replication of DNA essential.

<span class="mw-page-title-main">Polymerase</span> Class of enzymes which synthesize nucleic acid chains or polymers

In biochemistry, a polymerase is an enzyme that synthesizes long chains of polymers or nucleic acids. DNA polymerase and RNA polymerase are used to assemble DNA and RNA molecules, respectively, by copying a DNA template strand using base-pairing interactions or RNA by half ladder replication.

<span class="mw-page-title-main">Reverse transcriptase</span> Enzyme which generates DNA

A reverse transcriptase (RT) is an enzyme used to generate complementary DNA (cDNA) from an RNA template, a process termed reverse transcription. Reverse transcriptases are used by viruses such as HIV and hepatitis B to replicate their genomes, by retrotransposon mobile genetic elements to proliferate within the host genome, and by eukaryotic cells to extend the telomeres at the ends of their linear chromosomes. Contrary to a widely held belief, the process does not violate the flows of genetic information as described by the classical central dogma, as transfers of information from RNA to DNA are explicitly held possible.

<span class="mw-page-title-main">Transcription (biology)</span> Process of copying a segment of DNA into RNA

Transcription is the process of copying a segment of DNA into RNA. The segments of DNA transcribed into RNA molecules that can encode proteins produce messenger RNA (mRNA). Other segments of DNA are transcribed into RNA molecules called non-coding RNAs (ncRNAs).

<span class="mw-page-title-main">RNA polymerase</span> Enzyme that synthesizes RNA from DNA

In molecular biology, RNA polymerase, or more specifically DNA-directed/dependent RNA polymerase (DdRP), is an enzyme that catalyzes the chemical reactions that synthesize RNA from a DNA template.

<span class="mw-page-title-main">DNA polymerase</span> Form of DNA replication

A DNA polymerase is a member of a family of enzymes that catalyze the synthesis of DNA molecules from nucleoside triphosphates, the molecular precursors of DNA. These enzymes are essential for DNA replication and usually work in groups to create two identical DNA duplexes from a single original DNA duplex. During this process, DNA polymerase "reads" the existing DNA strands to create two new strands that match the existing ones. These enzymes catalyze the chemical reaction

<span class="mw-page-title-main">Helicase</span> Class of enzymes to unpack an organisms genes

Helicases are a class of enzymes thought to be vital to all organisms. Their main function is to unpack an organism's genetic material. Helicases are motor proteins that move directionally along a nucleic acid phosphodiester backbone, separating two hybridized nucleic acid strands, using energy from ATP hydrolysis. There are many helicases, representing the great variety of processes in which strand separation must be catalyzed. Approximately 1% of eukaryotic genes code for helicases.

<span class="mw-page-title-main">DNA polymerase I</span> Family of enzymes

DNA polymerase I is an enzyme that participates in the process of prokaryotic DNA replication. Discovered by Arthur Kornberg in 1956, it was the first known DNA polymerase. It was initially characterized in E. coli and is ubiquitous in prokaryotes. In E. coli and many other bacteria, the gene that encodes Pol I is known as polA. The E. coli Pol I enzyme is composed of 928 amino acids, and is an example of a processive enzyme — it can sequentially catalyze multiple polymerisation steps without releasing the single-stranded template. The physiological function of Pol I is mainly to support repair of damaged DNA, but it also contributes to connecting Okazaki fragments by deleting RNA primers and replacing the ribonucleotides with DNA.

DnaG is a bacterial DNA primase and is encoded by the dnaG gene. The enzyme DnaG, and any other DNA primase, synthesizes short strands of RNA known as oligonucleotides during DNA replication. These oligonucleotides are known as primers because they act as a starting point for DNA synthesis. DnaG catalyzes the synthesis of oligonucleotides that are 10 to 60 nucleotides long, however most of the oligonucleotides synthesized are 11 nucleotides. These RNA oligonucleotides serve as primers, or starting points, for DNA synthesis by bacterial DNA polymerase III. DnaG is important in bacterial DNA replication because DNA polymerase cannot initiate the synthesis of a DNA strand, but can only add nucleotides to a preexisting strand. DnaG synthesizes a single RNA primer at the origin of replication. This primer serves to prime leading strand DNA synthesis. For the other parental strand, the lagging strand, DnaG synthesizes an RNA primer every few kilobases (kb). These primers serve as substrates for the synthesis of Okazaki fragments.

<span class="mw-page-title-main">DNA polymerase III holoenzyme</span> Primary enzyme complex involved in prokaryotic DNA replication

DNA polymerase III holoenzyme is the primary enzyme complex involved in prokaryotic DNA replication. It was discovered by Thomas Kornberg and Malcolm Gefter in 1970. The complex has high processivity and, specifically referring to the replication of the E.coli genome, works in conjunction with four other DNA polymerases. Being the primary holoenzyme involved in replication activity, the DNA Pol III holoenzyme also has proofreading capabilities that corrects replication mistakes by means of exonuclease activity reading 3'→5' and synthesizing 5'→3'. DNA Pol III is a component of the replisome, which is located at the replication fork.

<span class="mw-page-title-main">Okazaki fragments</span> Transient components of lagging strand of DNA

Okazaki fragments are short sequences of DNA nucleotides which are synthesized discontinuously and later linked together by the enzyme DNA ligase to create the lagging strand during DNA replication. They were discovered in the 1960s by the Japanese molecular biologists Reiji and Tsuneko Okazaki, along with the help of some of their colleagues.

<span class="mw-page-title-main">Replisome</span> Molecular complex

The replisome is a complex molecular machine that carries out replication of DNA. The replisome first unwinds double stranded DNA into two single strands. For each of the resulting single strands, a new complementary sequence of DNA is synthesized. The total result is formation of two new double stranded DNA sequences that are exact copies of the original double stranded DNA sequence.

<span class="mw-page-title-main">RNA-dependent RNA polymerase</span> Enzyme that synthesizes RNA from an RNA template

RNA-dependent RNA polymerase (RdRp) or RNA replicase is an enzyme that catalyzes the replication of RNA from an RNA template. Specifically, it catalyzes synthesis of the RNA strand complementary to a given RNA template. This is in contrast to typical DNA-dependent RNA polymerases, which all organisms use to catalyze the transcription of RNA from a DNA template.

<span class="mw-page-title-main">Eukaryotic DNA replication</span> DNA replication in eukaryotic organisms

Eukaryotic DNA replication is a conserved mechanism that restricts DNA replication to once per cell cycle. Eukaryotic DNA replication of chromosomal DNA is central for the duplication of a cell and is necessary for the maintenance of the eukaryotic genome.

<span class="mw-page-title-main">PRIM2</span> Protein-coding gene in the species Homo sapiens

DNA primase large subunit is an enzyme that in humans is encoded by the PRIM2 gene.

<span class="mw-page-title-main">T7 DNA polymerase</span>

T7 DNA polymerase is an enzyme used during the DNA replication of the T7 bacteriophage. During this process, the DNA polymerase “reads” existing DNA strands and creates two new strands that match the existing ones. The T7 DNA polymerase requires a host factor, E. coli thioredoxin, in order to carry out its function. This helps stabilize the binding of the necessary protein to the primer-template to improve processivity by more than 100-fold, which is a feature unique to this enzyme. It is a member of the Family A DNA polymerases, which include E. coli DNA polymerase I and Taq DNA polymerase.

<span class="mw-page-title-main">PrimPol</span> Protein-coding gene in the species Homo sapiens

PrimPol is a protein encoded by the PRIMPOL gene in humans. PrimPol is a eukaryotic protein with both DNA polymerase and DNA Primase activities involved in translesion DNA synthesis. It is the first eukaryotic protein to be identified with priming activity using deoxyribonucleotides. It is also the first protein identified in the mitochondria to have translesion DNA synthesis activities.

<span class="mw-page-title-main">PRIM1</span> Protein-coding gene in the species Homo sapiens

DNA primase small subunit is an enzyme that in humans is encoded by the PRIM1 gene.

<span class="mw-page-title-main">DNA polymerase alpha catalytic subunit</span> Protein-coding gene in humans

DNA polymerase alpha catalytic subunit is an enzyme that in humans is encoded by the POLA1 gene.

A helicase–primase complex is a complex of enzymes including DNA helicase and DNA primase. A helicase-primase associated factor protein may also be present.

References

  1. ↑ Bocquier AA, Liu L, Cann IK, Komori K, Kohda D, Ishino Y (March 2001). "Archaeal primase: bridging the gap between RNA and DNA polymerases". Current Biology. 11 (6): 452–6. doi: 10.1016/s0960-9822(01)00119-1 . PMID   11301257.
  2. 1 2 Baranovskiy AG, Zhang Y, Suwa Y, Babayeva ND, Gu J, Pavlov YI, Tahirov TH (February 2015). "Crystal structure of the human primase". The Journal of Biological Chemistry. 290 (9): 5635–46. doi: 10.1074/jbc.M114.624742 . PMC   4342476 . PMID   25550159.
  3. 1 2 3 Griep MA (August 1995). "Primase structure and function". Indian Journal of Biochemistry & Biophysics. 32 (4): 171–8. PMID   8655184.
  4. 1 2 3 4 5 6 7 Keck JL, Roche DD, Lynch AS, Berger JM (March 2000). "Structure of the RNA polymerase domain of E. coli primase". Science. 287 (5462): 2482–6. Bibcode:2000Sci...287.2482K. doi:10.1126/science.287.5462.2482. PMID   10741967.
  5. 1 2 3 Lee JB, Hite RK, Hamdan SM, Xie XS, Richardson CC, van Oijen AM (February 2006). "DNA primase acts as a molecular brake in DNA replication" (PDF). Nature. 439 (7076): 621–4. Bibcode:2006Natur.439..621L. doi:10.1038/nature04317. PMID   16452983. S2CID   3099842.
  6. 1 2 3 4 Cavanaugh NA, Kuchta RD (January 2009). "Initiation of new DNA strands by the herpes simplex virus-1 primase-helicase complex and either herpes DNA polymerase or human DNA polymerase alpha". The Journal of Biological Chemistry. 284 (3): 1523–32. doi: 10.1074/jbc.M805476200 . PMC   2615532 . PMID   19028696.
  7. ↑ Keck JL, Berger JM (January 2001). "Primus inter pares (first among equals)". Nature Structural Biology. 8 (1): 2–4. doi:10.1038/82996. PMID   11135655. S2CID   17108681.
  8. 1 2 Aravind L, Leipe DD, Koonin EV (September 1998). "Toprim--a conserved catalytic domain in type IA and II topoisomerases, DnaG-type primases, OLD family nucleases and RecR proteins". Nucleic Acids Research. 26 (18): 4205–13. doi:10.1093/nar/26.18.4205. PMC   147817 . PMID   9722641.
  9. ↑ Hou L, Klug G, Evguenieva-Hackenberg E (March 2013). "The archaeal DnaG protein needs Csl4 for binding to the exosome and enhances its interaction with adenine-rich RNAs". RNA Biology. 10 (3): 415–24. doi:10.4161/rna.23450. PMC   3672285 . PMID   23324612.
  10. ↑ Iyer LM, Koonin EV, Leipe DD, Aravind L (2005). "Origin and evolution of the archaeo-eukaryotic primase superfamily and related palm-domain proteins: structural insights and new members". Nucleic Acids Research. 33 (12): 3875–96. doi:10.1093/nar/gki702. PMC   1176014 . PMID   16027112.
  11. 1 2 3 Lao-Sirieix SH, Bell SD (December 2004). "The heterodimeric primase of the hyperthermophilic archaeon Sulfolobus solfataricus possesses DNA and RNA primase, polymerase and 3'-terminal nucleotidyl transferase activities". Journal of Molecular Biology. 344 (5): 1251–63. doi:10.1016/j.jmb.2004.10.018. PMID   15561142.
  12. 1 2 3 4 Guilliam TA, Keen BA, Brissett NC, Doherty AJ (August 2015). "Primase-polymerases are a functionally diverse superfamily of replication and repair enzymes". Nucleic Acids Research. 43 (14): 6651–64. doi:10.1093/nar/gkv625. PMC   4538821 . PMID   26109351.
  13. 1 2 3 4 Gill S, Krupovic M, Desnoues N, Béguin P, Sezonov G, Forterre P (April 2014). "A highly divergent archaeo-eukaryotic primase from the Thermococcus nautilus plasmid, pTN2". Nucleic Acids Research. 42 (6): 3707–19. doi:10.1093/nar/gkt1385. PMC   3973330 . PMID   24445805.
  14. 1 2 3 4 Kazlauskas D, Sezonov G, Charpin N, Venclovas Č, Forterre P, Krupovic M (March 2018). "Novel Families of Archaeo-Eukaryotic Primases Associated with Mobile Genetic Elements of Bacteria and Archaea". Journal of Molecular Biology. 430 (5): 737–750. doi:10.1016/j.jmb.2017.11.014. PMC   5862659 . PMID   29198957.
  15. 1 2 Wan L, Lou J, Xia Y, Su B, Liu T, Cui J, Sun Y, Lou H, Huang J (December 2013). "hPrimpol1/CCDC111 is a human DNA primase-polymerase required for the maintenance of genome integrity". EMBO Reports. 14 (12): 1104–12. doi:10.1038/embor.2013.159. PMC   3981091 . PMID   24126761.
  16. 1 2 3 García-Gómez S, Reyes A, Martínez-Jiménez MI, Chocrón ES, Mourón S, Terrados G, Powell C, Salido E, Méndez J, Holt IJ, Blanco L (November 2013). "PrimPol, an archaic primase/polymerase operating in human cells". Molecular Cell. 52 (4): 541–53. doi:10.1016/j.molcel.2013.09.025. PMC   3899013 . PMID   24207056.
  17. 1 2 Sanchez-Berrondo J, Mesa P, Ibarra A, Martínez-Jiménez MI, Blanco L, Méndez J, Boskovic J, Montoya G (February 2012). "Molecular architecture of a multifunctional MCM complex". Nucleic Acids Research. 40 (3): 1366–80. doi:10.1093/nar/gkr831. PMC   3273815 . PMID   21984415.
  18. 1 2 Keen BA, Jozwiakowski SK, Bailey LJ, Bianchi J, Doherty AJ (May 2014). "Molecular dissection of the domain architecture and catalytic activities of human PrimPol". Nucleic Acids Research. 42 (9): 5830–45. doi:10.1093/nar/gku214. PMC   4027207 . PMID   24682820.
  19. ↑ Jozwiakowski SK, Borazjani Gholami F, Doherty AJ (February 2015). "Archaeal replicative primases can perform translesion DNA synthesis". Proceedings of the National Academy of Sciences of the United States of America. 112 (7): E633-8. Bibcode:2015PNAS..112E.633J. doi: 10.1073/pnas.1412982112 . PMC   4343091 . PMID   25646444.
  20. ↑ Barry ER, Bell SD (December 2006). "DNA replication in the archaea". Microbiology and Molecular Biology Reviews. 70 (4): 876–87. doi:10.1128/MMBR.00029-06. PMC   1698513 . PMID   17158702.
  21. ↑ Lao-Sirieix SH, Pellegrini L, Bell SD (October 2005). "The promiscuous primase". Trends in Genetics. 21 (10): 568–72. doi:10.1016/j.tig.2005.07.010. PMID   16095750.
  22. 1 2 3 Kazlauskas D, Krupovic M, Venclovas Č (June 2016). "The logic of DNA replication in double-stranded DNA viruses: insights from global analysis of viral genomes". Nucleic Acids Research. 44 (10): 4551–64. doi:10.1093/nar/gkw322. PMC   4889955 . PMID   27112572.
  23. ↑ Lipps G, Weinzierl AO, von Scheven G, Buchen C, Cramer P (February 2004). "Structure of a bifunctional DNA primase-polymerase". Nature Structural & Molecular Biology. 11 (2): 157–62. doi:10.1038/nsmb723. PMID   14730355. S2CID   25123984.
This page is based on this Wikipedia article
Text is available under the CC BY-SA 4.0 license; additional terms may apply.
Images, videos and audio are available under their respective licenses.