Fertility factor (bacteria)

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The fertility factor (first named F by one of its discoverers Esther Lederberg; also called the sex factor in E. coli or the F sex factor; also called F-plasmid) [1] [2] [3] allows genes to be transferred from one bacterium carrying the factor to another bacterium lacking the factor by conjugation. The F factor was the first plasmid to be discovered. Unlike other plasmids, F factor is constitutive for transfer proteins due to a mutation in the gene finO. [4] The F plasmid belongs to a class of conjugative plasmids that control sexual functions of bacteria with a fertility inhibition (Fin) system.

Contents

Discovery

Esther M. Lederberg and Luigi L. Cavalli-Sforza discovered "F," [5] subsequently publishing with Joshua Lederberg. [6] Once her results were announced, two other labs joined the studies. "This was not a simultaneous independent discovery of F (I names as Fertility Factor until it was understood.) We wrote to Hayes, Jacob, & Wollman who then proceeded with their studies." [7] The discovery of "F" has sometimes been confused with William Hayes' discovery of "sex factor", though he never claimed priority. Indeed, "he [Hayes] thought F was really lambda, and when we convinced him [that it was not], he then began his work." [8]

Structure

The most common functional segments constituting F factors are: [9]

Some F plasmid genes and their Function:

Relation to the genome

The episome that harbors the F factor can exist as an independent plasmid or integrate into the bacterial cell's genome. There are several names for the possible states:

Function

When an F+ cell conjugates/mates with an F− cell, the result is two F+ cells, both capable of transmitting the plasmid to other F− cells by conjugation. A pilus on the F+ cell interacts with the recipient cell allowing formation of a mating junction, the DNA is nicked on one strand, unwound and transferred to the recipient. [3] [9]

The F-plasmid belongs to a class of conjugative plasmids that control sexual functions of bacteria with a fertility inhibition (Fin) system. In this system, a trans-acting factor, FinO, and antisense RNAs, FinP, combine to repress the expression of the activator gene TraJ. TraJ is a transcription factor that upregulates the tra operon. The tra operon includes genes required for conjugation and plasmid transfer. This means that an F+ bacteria can always act as a donor cell. The finO gene of the original F plasmid (in E. coli K12) is interrupted by an IS3 insertion, resulting in constitutive tra operon expression. [11] [12] F+ cells also have the surface exclusion proteins TraS and TraT on the bacterial surface. These proteins prevent secondary mating events involving plasmids belonging to the same incompatibility (Inc) group. Thus, each F+ bacterium can host only a single plasmid type of any given incompatibility group.

In the case of Hfr transfer, the resulting transconjugates are rarely Hfr. The result of Hfr/F− conjugation is a F− strain with a new genotype. When F-prime plasmids are transferred to a recipient bacterial cell, they carry pieces of the donor's DNA that can become important in recombination. Bioengineers have created F plasmids that can contain inserted foreign DNA; this is called a bacterial artificial chromosome.

The first DNA helicase ever described is encoded on the F-plasmid and is responsible for initiating plasmid transfer. It was originally called E. coli DNA Helicase I, but is now known as F-plasmid TraI. In addition to being a helicase, the 1756 amino acid (one of the largest in E. coli) F-plasmid TraI protein is also responsible for both specific and non-specific single-stranded DNA binding as well as catalyzing the nicking of single-stranded DNA at the origin of transfer.

See also

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<span class="mw-page-title-main">Hfr cell</span>


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References

  1. ↑ Dugger, Gordon (1976). A dictionary of life sciences. (London [usw.]): Macmillan). p. 130. ISBN   978-0333194362.
  2. ↑ Hine, Robert (2008). A dictionary of biology (6th ed.). Oxford: Oxford University Press. p. 592. ISBN   9780199204625.
  3. 1 2 Lawley, TD; Klimke, WA; Gubbins, MJ; Frost, LS (15 July 2003). "F factor conjugation is a true type IV secretion system". FEMS Microbiology Letters. 224 (1): 1–15. doi: 10.1016/S0378-1097(03)00430-0 . PMID   12855161.
  4. ↑ Yoshioka, Y; Ohtsubo, H; Ohtsubo, E (1987). "Repressor gene finO in plasmids R100 and F: constitutive transfer of plasmid F is caused by insertion of IS3 into F finO". Journal of Bacteriology. 169 (2): 619–623. doi:10.1128/jb.169.2.619-623.1987. ISSN   0021-9193. PMC   211823 . PMID   3027040.
  5. ↑ As written by Esther Lederberg: "At this same time, L. Cavalli in Milan Italy, discovered the phenomenon of sterility from a different angle. Exchange of data showed that if I had done an experiment, he had planned to do it, but had completed another that we had planned. So we decided to pool forces and collaborate." See http://www.estherMlederberg.com/Clark_MemorialVita/HISTORY52.html
  6. ↑ Lederberg, J., Cavalli, L. L., and Lederberg, E. M., Nov. 1952, "Sex compatibility in Escherichia coli", Genetics 37(6):720-730
  7. ↑ "Historical Notes About Fertility Factor F (version B)". www.esthermlederberg.com. Retrieved 2023-07-14.
  8. ↑ "Historical Notes About Fertility Factor F (version A)". www.esthermlederberg.com. Retrieved 2023-07-14.
  9. 1 2 Arutyunov, Denis; Frost, Laura S. (2013-07-01). "F conjugation: Back to the beginning". Plasmid. 70 (1): 18–32. doi:10.1016/j.plasmid.2013.03.010. ISSN   0147-619X. PMID   23632276.
  10. ↑ Hartwell, Leland; Leroy Hood; Michael L. Goldberg; Ann E. Reynolds; Lee M. Silver (2011). Genetics:From Genes to Genomes; Fourth Edition. New York, NY: McGraw-Hill. ISBN   978-0-07-352526-6.
  11. ↑ Jerome, LJ; van Biesen T; Frost LS (1999). "Degradation of FinP antisense RNA from F-like plasmids: the RNA-binding protein, FinO, protects FinP from ribonuclease E". J Mol Biol. 285 (4): 1457–1473. doi:10.1006/jmbi.1998.2404. PMID   9917389.
  12. ↑ Arthur DC, Ghetu AF, Gubbins MJ, Edwards RA, Frost LS, Glover JN (2003). "FinO is an RNA chaperone that facilitates sense-antisense RNA interactions". EMBO J. 22 (23): 6346–55. doi:10.1093/emboj/cdg607. PMC   291848 . PMID   14633993.
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