Charles Kurland

Last updated
Charles Kurland
Born
Charles Gabriel Kurland

(1936-01-14) 14 January 1936 (age 88)
CitizenshipAmerican and Swedish
Education Harvard
Known forBiochemistry and biophysics of the ribosome
Scientific career
FieldsBiochemistry
Institutions Copenhagen University, Uppsala University, Lund University
Doctoral advisor James D. Watson

Charles Gabriel Kurland (born 14 January 1936) is an American-born Swedish biochemist.

Contents

Kurland earned a doctorate in 1961 at Harvard University, advised by James D. Watson. [1] [2] Kurland accepted a postdoctoral research position at the Microbiology Institute of the University of Copenhagen, then joined the Uppsala University faculty in 1971. [2] He retired from Uppsala in 2001, and was granted emeritus status. [3] He was later affiliated with Lund University. [2] [4] [5]

Research

Kurland's doctoral work dealt the structure of RNA, [6] and continued with the discovery of messenger RNA (mRNA), work that also involved François Gros, Walter Gilbert and James Watson. [7] This was published simultaneously with the report by Sydney Brenner, François Jacob and Matthew Meselson of the same discovery. [8] It was followed by numerous papers concerned with ribosomal proteins [9] [10]

In the later part of his career Kurland has been interested in the origins of mitochondria [11] and the tree of life. [12]

Academy memberships

Kurland was elected to the Royal Swedish Academy of Sciences in 1988 as a foreign member, and reclassified as a Swedish member in 2002. [13] The Estonian Academy of Sciences recognized his achievements in biochemistry, and awarded Kurland an equivalent honor in 1991. [3]

Related Research Articles

<span class="mw-page-title-main">Ribosome</span> Synthesizes proteins in cells

Ribosomes are macromolecular machines, found within all cells, that perform biological protein synthesis. Ribosomes link amino acids together in the order specified by the codons of messenger RNA molecules to form polypeptide chains. Ribosomes consist of two major components: the small and large ribosomal subunits. Each subunit consists of one or more ribosomal RNA molecules and many ribosomal proteins. The ribosomes and associated molecules are also known as the translational apparatus.

<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">Marshall Warren Nirenberg</span> American biochemist and geneticist

Marshall Warren Nirenberg was an American biochemist and geneticist. He shared a Nobel Prize in Physiology or Medicine in 1968 with Har Gobind Khorana and Robert W. Holley for "breaking the genetic code" and describing how it operates in protein synthesis. In the same year, together with Har Gobind Khorana, he was awarded the Louisa Gross Horwitz Prize from Columbia University. His most famous discovery came when he coined the phrase “The mitochondria is the powerhouse of the cell.”

The Shine–Dalgarno (SD) sequence is a ribosomal binding site in bacterial and archaeal messenger RNA, generally located around 8 bases upstream of the start codon AUG. The RNA sequence helps recruit the ribosome to the messenger RNA (mRNA) to initiate protein synthesis by aligning the ribosome with the start codon. Once recruited, tRNA may add amino acids in sequence as dictated by the codons, moving downstream from the translational start site.

<span class="mw-page-title-main">Ribosomal RNA</span> RNA component of the ribosome, essential for protein synthesis in all living organisms

Ribosomal ribonucleic acid (rRNA) is a type of non-coding RNA which is the primary component of ribosomes, essential to all cells. rRNA is a ribozyme which carries out protein synthesis in ribosomes. Ribosomal RNA is transcribed from ribosomal DNA (rDNA) and then bound to ribosomal proteins to form small and large ribosome subunits. rRNA is the physical and mechanical factor of the ribosome that forces transfer RNA (tRNA) and messenger RNA (mRNA) to process and translate the latter into proteins. Ribosomal RNA is the predominant form of RNA found in most cells; it makes up about 80% of cellular RNA despite never being translated into proteins itself. Ribosomes are composed of approximately 60% rRNA and 40% ribosomal proteins, though this ratio differs between prokaryotes and eukaryotes.

<span class="mw-page-title-main">Transfer-messenger RNA</span>

Transfer-messenger RNA is a bacterial RNA molecule with dual tRNA-like and messenger RNA-like properties. The tmRNA forms a ribonucleoprotein complex (tmRNP) together with Small Protein B (SmpB), Elongation Factor Tu (EF-Tu), and ribosomal protein S1. In trans-translation, tmRNA and its associated proteins bind to bacterial ribosomes which have stalled in the middle of protein biosynthesis, for example when reaching the end of a messenger RNA which has lost its stop codon. The tmRNA is remarkably versatile: it recycles the stalled ribosome, adds a proteolysis-inducing tag to the unfinished polypeptide, and facilitates the degradation of the aberrant messenger RNA. In the majority of bacteria these functions are carried out by standard one-piece tmRNAs. In other bacterial species, a permuted ssrA gene produces a two-piece tmRNA in which two separate RNA chains are joined by base-pairing.

Bacterial translation is the process by which messenger RNA is translated into proteins in bacteria.


Arthur Beck Pardee was an American biochemist. One biographical portrait begins "Among the titans of science, Arthur Pardee is especially intriguing." There is hardly a field of molecular biology that is not affected by his work, which has advanced our understanding through theoretical predictions followed by insightful experiments. He is perhaps most famous for his part in the 'PaJaMo experiment' of the late 1950s, which greatly helped in the discovery of messenger RNA. He is also well known as the discoverer of the restriction point, in which a cell commits itself to certain cell cycle events during the G1 cycle. He did a great deal of work on tumor growth and regulation, with a particular focus on the role of estrogen in hormone-responsive tumors. He is also well known for the development of various biochemical research techniques, most notably the differential display methodology, which is used in examining the activation of genes in cells. More recently he championed the acceptance and adoption of the conceptual review as a valuable approach to unearthing new knowledge from the enormous stores of information in the scientific literature. He died in February 2019 at the age of 97.

<span class="mw-page-title-main">Ribosome recycling factor</span> Protein found in bacterial cells, mitochondria, and chloroplasts

Ribosome recycling factor or ribosome release factor (RRF) is a protein found in bacterial cells as well as eukaryotic organelles, specifically mitochondria and chloroplasts. It functions to recycle ribosomes after completion of protein synthesis. In humans, the mitochrondrial version is coded by the MRRF gene.

<span class="mw-page-title-main">Ribosomal protein</span> Proteins found in ribosomes

A ribosomal protein is any of the proteins that, in conjunction with rRNA, make up the ribosomal subunits involved in the cellular process of translation. E. coli, other bacteria and Archaea have a 30S small subunit and a 50S large subunit, whereas humans and yeasts have a 40S small subunit and a 60S large subunit. Equivalent subunits are frequently numbered differently between bacteria, Archaea, yeasts and humans.

A bacterial initiation factor (IF) is a protein that stabilizes the initiation complex for polypeptide translation.

Elongation factor 4 (EF-4) is an elongation factor that is thought to back-translocate on the ribosome during the translation of RNA to proteins. It is found near-universally in bacteria and in eukaryotic endosymbiotic organelles including the mitochondria and the plastid. Responsible for proofreading during protein synthesis, EF-4 is a recent addition to the nomenclature of bacterial elongation factors.

<span class="mw-page-title-main">5S ribosomal RNA</span> RNA component of the large subunit of the ribosome

The 5S ribosomal RNA is an approximately 120 nucleotide-long ribosomal RNA molecule with a mass of 40 kDa. It is a structural and functional component of the large subunit of the ribosome in all domains of life, with the exception of mitochondrial ribosomes of fungi and animals. The designation 5S refers to the molecule's sedimentation coefficient in an ultracentrifuge, which is measured in Svedberg units (S).

<span class="mw-page-title-main">Mitochondrial ribosome</span> Protein complex

The mitochondrial ribosome, or mitoribosome, is a protein complex that is active in mitochondria and functions as a riboprotein for translating mitochondrial mRNAs encoded in mtDNA. The mitoribosome is attached to the inner mitochondrial membrane. Mitoribosomes, like cytoplasmic ribosomes, consist of two subunits — large (mt-LSU) and small (mt-SSU). Mitoribosomes consist of several specific proteins and fewer rRNAs. While mitochondrial rRNAs are encoded in the mitochondrial genome, the proteins that make up mitoribosomes are encoded in the nucleus and assembled by cytoplasmic ribosomes before being implanted into the mitochondria.

Small subunit ribosomal ribonucleic acid is the smaller of the two major RNA components of the ribosome. Associated with a number of ribosomal proteins, the SSU rRNA forms the small subunit of the ribosome. It is encoded by SSU-rDNA.

Large subunit ribosomal ribonucleic acid is the largest of the two major RNA components of the ribosome. Associated with a number of ribosomal proteins, the LSU rRNA forms the large subunit of the ribosome. The LSU rRNA acts as a ribozyme, catalyzing peptide bond formation.

<span class="mw-page-title-main">50S ribosomal protein L25</span>

50S ribosomal protein L25 is a protein that in Escherichia coli is encoded by the rplY gene.

<span class="mw-page-title-main">François Gros</span> French biologist (1925–2022)

François Gros was a French biologist and one of the pioneers of cellular biochemistry in France. His scientific career concerned genes and their role in regulating cellular functions.

Lynn Dalgarno is an Australian geneticist known for the discovery of the Shine–Dalgarno sequence with his graduate student, John Shine.

David Schlessinger is a Canadian-born American biochemist, microbiologist, and geneticist. He is known for his directorship of the development of the map of the X chromosome.

References

  1. "Kurland, Charles, 1967 September 15-1974 May 22, 1967 September 15-1974 May 22". Harvard University. Retrieved 10 March 2022.
  2. 1 2 3 "Charles G. Kurland" (PDF). Annual International Gene Forum. 15 September 2001. Archived from the original (PDF) on 17 June 2016. Retrieved 10 March 2022.
  3. 1 2 "Charles Gabriel Kurland". Estonian Academy of Sciences. Retrieved 10 March 2022.
  4. "Våra förfäder var glupska eukaryoter". Forskning (in Swedish). 29 May 2006. Retrieved 10 March 2022.
  5. "Charles Kurland". Lund University. Retrieved 10 March 2022.
  6. Kurland, C.G. (1960). "Molecular characterization of ribonucleic acid from Escherichia coli ribosomes: I. Isolation and molecular weights". J. Molec. Biol. 1 (2): 83–91. doi:10.1016/S0022-2836(60)80029-0.
  7. Gros, François; Hiatt, H.; Gilbert, Walter; Kurland, C.; Risebrough, R. W.; Watson, J. D. (1961). "Unstable ribonucleic acid revealed by pulse labelling of Escherichia coli". Nature. 190 (4776): 581–585. doi:10.1038/190581a0.
  8. Brenner, S.; Jacob, F.; Meselson, M. (1961). "An unstable intermediate carrying information from genes to ribosomes for protein synthesis". Nature. 190 (4776): 576–581. doi:10.1038/190576a0.
  9. Hardy, S. J. S.; Kurland, C. G.; Voynow, P.; Mora, G. (1969). "Ribosomal proteins of Escherichia coli. I. Purification of the 30 S ribosomal proteins". Biochemistry. 8 (7): 2897–2905. doi:10.1021/bi00835a031.
  10. Gary, R.; Craven, P.; Hardy, S. J. S.; Kurland, C. G. (1969). "Ribosomal proteins of Escherichia coli. II. Chemical and physical characterization of the 30 S ribosomal proteins". Biochemistry. 8 (7): 2906–2915. doi:10.1021/bi00835a032.
  11. Harish, Ajith; Kurland, C. G. (2017). "Mitochondria are not captive bacteria". J. Theor. Biol. 434: 88–98. doi:10.1016/j.jtbi.2017.07.011.
  12. Harish, Ajith; Kurland, C. G. (2017). "Akaryotes and Eukaryotes are independent descendants of a universal common ancestor". Biochimie. 138: 168–183. doi:10.1016/j.biochi.2017.04.013.
  13. "Charles Kurland". Royal Swedish Academy of Sciences. Retrieved 10 March 2022.