Literature DB >> 9000619

Regulation of the activity of the type IC EcoR124I restriction enzyme.

E M Kulik1, T A Bickle.   

Abstract

Restriction-modification (R-M) systems must regulate the expression of their genes so that the chromosomal genome is modified at all times by the methyltransferase to protect the host cell from the potential lethal action of the cognate restriction endonuclease. Since type I R-M systems can be transferred to non-modified Escherichia coli cells by conjugation or transformation without killing the recipient, they must have some means to regulate their restriction activity upon entering a new host cell to avoid restriction of unprotected host DNA and cell death. This is especially true for EcoR124I, a type IC family member, which is coded for by a conjugative plasmid. Control of EcoR124I restriction activity is most likely at the post-translational level as the transfer of the EcoR124I system into a recipient cell that already expressed the HsdR subunit of this system was not a lethal event. Additionally, the kinetics of restriction activity upon transfer of the genes coding for the EcoR124I RM system to a recipient cell are the same, irrespective of the modification state of the recipient cell or the presence or absence of the EcoR124I HsdR subunit in the new host cells. The mechanism controlling the restriction activity of a type IC R-M system upon transfer to a new host cell is different from that controlling the chromosomally coded type IA and IB R-M systems. The previously discovered hsdC mutant, which affects the establishment of the type IA system EcoKI, was shown to affect the establishment of the type IB system EcoAI, but to have no influence on EcoR124I.

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Year:  1996        PMID: 9000619     DOI: 10.1006/jmbi.1996.0685

Source DB:  PubMed          Journal:  J Mol Biol        ISSN: 0022-2836            Impact factor:   5.469


  14 in total

1.  Regulation of endonuclease activity by proteolysis prevents breakage of unmodified bacterial chromosomes by type I restriction enzymes.

Authors:  S Makovets; V A Doronina; N E Murray
Journal:  Proc Natl Acad Sci U S A       Date:  1999-08-17       Impact factor: 11.205

2.  Cellular responses to postsegregational killing by restriction-modification genes.

Authors:  N Handa; A Ichige; K Kusano; I Kobayashi
Journal:  J Bacteriol       Date:  2000-04       Impact factor: 3.490

Review 3.  Type I restriction systems: sophisticated molecular machines (a legacy of Bertani and Weigle).

Authors:  N E Murray
Journal:  Microbiol Mol Biol Rev       Date:  2000-06       Impact factor: 11.056

Review 4.  Behavior of restriction-modification systems as selfish mobile elements and their impact on genome evolution.

Authors:  I Kobayashi
Journal:  Nucleic Acids Res       Date:  2001-09-15       Impact factor: 16.971

Review 5.  Nucleoside triphosphate-dependent restriction enzymes.

Authors:  D T Dryden; N E Murray; D N Rao
Journal:  Nucleic Acids Res       Date:  2001-09-15       Impact factor: 16.971

6.  Maintenance forced by a restriction-modification system can be modulated by a region in its modification enzyme not essential for methyltransferase activity.

Authors:  Satona Ohno; Naofumi Handa; Miki Watanabe-Matsui; Noriko Takahashi; Ichizo Kobayashi
Journal:  J Bacteriol       Date:  2008-01-11       Impact factor: 3.490

7.  A family of phase-variable restriction enzymes with differing specificities generated by high-frequency gene rearrangements.

Authors:  K Dybvig; R Sitaraman; C T French
Journal:  Proc Natl Acad Sci U S A       Date:  1998-11-10       Impact factor: 11.205

8.  The restriction-modification genes of Escherichia coli K-12 may not be selfish: they do not resist loss and are readily replaced by alleles conferring different specificities.

Authors:  M O'Neill; A Chen; N E Murray
Journal:  Proc Natl Acad Sci U S A       Date:  1997-12-23       Impact factor: 11.205

Review 9.  Diverse functions of restriction-modification systems in addition to cellular defense.

Authors:  Kommireddy Vasu; Valakunja Nagaraja
Journal:  Microbiol Mol Biol Rev       Date:  2013-03       Impact factor: 11.056

10.  Crystal structure of the Fic (Filamentation induced by cAMP) family protein SO4266 (gi|24375750) from Shewanella oneidensis MR-1 at 1.6 A resolution.

Authors:  Debanu Das; S Sri Krishna; Daniel McMullan; Mitchell D Miller; Qingping Xu; Polat Abdubek; Claire Acosta; Tamara Astakhova; Herbert L Axelrod; Prasad Burra; Dennis Carlton; Hsiu-Ju Chiu; Thomas Clayton; Marc C Deller; Lian Duan; Ylva Elias; Marc-André Elsliger; Dustin Ernst; Julie Feuerhelm; Anna Grzechnik; Slawomir K Grzechnik; Joanna Hale; Gye Won Han; Lukasz Jaroszewski; Kevin K Jin; Heath E Klock; Mark W Knuth; Piotr Kozbial; Abhinav Kumar; David Marciano; Andrew T Morse; Kevin D Murphy; Edward Nigoghossian; Linda Okach; Silvya Oommachen; Jessica Paulsen; Ron Reyes; Christopher L Rife; Natasha Sefcovic; Henry Tien; Christine B Trame; Christina V Trout; Henry van den Bedem; Dana Weekes; Aprilfawn White; Keith O Hodgson; John Wooley; Ashley M Deacon; Adam Godzik; Scott A Lesley; Ian A Wilson
Journal:  Proteins       Date:  2009-04
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