Convergent Evolution of the Barnase/EndoU/Colicin/RelE (BECR) Fold in Antibacterial tRNase Toxins.

Item request has been placed! ×
Item request cannot be made. ×
loading   Processing Request
Read More Add to Saved list
  • Additional Information
    • Source:
      Publisher: Cell Press Country of Publication: United States NLM ID: 101087697 Publication Model: Print-Electronic Cited Medium: Internet ISSN: 1878-4186 (Electronic) Linking ISSN: 09692126 NLM ISO Abbreviation: Structure Subsets: MEDLINE
    • Publication Information:
      Publication: 2000- : Cambridge, Mass. : Cell Press
      Original Publication: London : Current Biology, c1993-
    • Subject Terms:
      Evolution, Molecular* ; Toxin-Antitoxin Systems*; Bacterial Proteins/*chemistry ; Bacterial Toxins/*chemistry ; Colicins/*chemistry ; Escherichia coli Proteins/*chemistry ; Membrane Proteins/*chemistry ; Ribonucleases/*chemistry; Bacterial Proteins/genetics ; Bacterial Proteins/metabolism ; Bacterial Toxins/genetics ; Bacterial Toxins/metabolism ; Binding Sites ; Colicins/genetics ; Colicins/metabolism ; Escherichia coli ; Escherichia coli Proteins/genetics ; Escherichia coli Proteins/metabolism ; Klebsiella pneumoniae/enzymology ; Klebsiella pneumoniae/genetics ; Membrane Proteins/genetics ; Membrane Proteins/metabolism ; Protein Binding ; RNA, Transfer/chemistry ; RNA, Transfer/metabolism ; Ribonucleases/genetics ; Ribonucleases/metabolism
    • Abstract:
      Contact-dependent growth inhibition (CDI) is a form of interbacterial competition mediated by CdiB-CdiA two-partner secretion systems. CdiA effector proteins carry polymorphic C-terminal toxin domains (CdiA-CT), which are neutralized by specific CdiI immunity proteins to prevent self-inhibition. Here, we present the crystal structures of CdiA-CT⋅CdiI complexes from Klebsiella pneumoniae 342 and Escherichia coli 3006. The toxins adopt related folds that resemble the ribonuclease domain of colicin D, and both are isoacceptor-specific tRNases that cleave the acceptor stem of deacylated tRNA GAU Ile . Although the toxins are similar in structure and substrate specificity, CdiA-CT Kp342 activity requires translation factors EF-Tu and EF-Ts, whereas CdiA-CT EC3006 is intrinsically active. Furthermore, the corresponding immunity proteins are unrelated in sequence and structure. CdiI Kp342 forms a dimeric β sandwich, whereas CdiI EC3006 is an α-solenoid monomer. Given that toxin-immunity genes co-evolve as linked pairs, these observations suggest that the similarities in toxin structure and activity reflect functional convergence.
      (Copyright © 2019 Elsevier Ltd. All rights reserved.)
    • Comments:
      Comment in: Structure. 2019 Nov 5;27(11):1613-1614. (PMID: 31693909)
    • References:
      Cell Mol Life Sci. 2010 May;67(9):1447-63. (PMID: 20155482)
      Structure. 1999 Feb 15;7(2):143-56. (PMID: 10368282)
      Curr Opin Struct Biol. 2014 Jun;26:92-103. (PMID: 24952217)
      Nucleic Acids Res. 2010 Jul;38(Web Server issue):W545-9. (PMID: 20457744)
      Mol Microbiol. 2018 Aug;109(4):509-527. (PMID: 29923643)
      Science. 2012 May 25;336(6084):1030-3. (PMID: 22628654)
      Proc Natl Acad Sci U S A. 2011 May 3;108(18):7403-7. (PMID: 21502523)
      Acta Crystallogr D Biol Crystallogr. 2011 Apr;67(Pt 4):235-42. (PMID: 21460441)
      Nucleic Acids Res. 2012 Aug;40(15):7016-45. (PMID: 22638584)
      Elife. 2017 Jul 11;6:. (PMID: 28696203)
      Methods Mol Biol. 1996;57:177-91. (PMID: 8850005)
      Nucleic Acids Res. 2017 May 19;45(9):5013-5025. (PMID: 28398546)
      Nucleic Acids Res. 2004 Jul 1;32(Web Server issue):W615-9. (PMID: 15215462)
      Proc Natl Acad Sci U S A. 2013 Apr 23;110(17):7032-7. (PMID: 23572593)
      J Comput Chem. 2004 Oct;25(13):1605-12. (PMID: 15264254)
      Genes Dev. 2012 Mar 1;26(5):515-25. (PMID: 22333533)
      PLoS Genet. 2016 Jun 29;12(6):e1006145. (PMID: 27355474)
      Proc Natl Acad Sci U S A. 2012 Dec 26;109(52):21480-5. (PMID: 23236156)
      Methods Mol Biol. 2009;498:105-15. (PMID: 18988021)
      PLoS Pathog. 2014 Apr 17;10(4):e1004076. (PMID: 24743836)
      Acta Crystallogr D Biol Crystallogr. 1997 May 1;53(Pt 3):240-55. (PMID: 15299926)
      MBio. 2017 Mar 28;8(2):. (PMID: 28351921)
      Biochemistry. 2013 Dec 3;52(48):8633-42. (PMID: 24251350)
      Biol Direct. 2012 Jun 25;7:18. (PMID: 22731697)
      J Mol Biol. 2015 Nov 20;427(23):3766-84. (PMID: 26449640)
      Science. 1999 Mar 26;283(5410):2097-100. (PMID: 10092236)
      J Mol Biol. 2009 Nov 27;394(2):251-67. (PMID: 19761774)
      Nucleic Acids Res. 2016 Feb 18;44(3):1256-70. (PMID: 26740583)
      Nucleic Acids Res. 2011 Jun;39(11):4532-52. (PMID: 21306995)
      Mol Microbiol. 2012 May;84(3):516-29. (PMID: 22435733)
      Cell. 2018 Nov 1;175(4):921-933.e14. (PMID: 30388452)
      Biochemistry. 1990 May 8;29(18):4268-77. (PMID: 2190631)
      Nat Commun. 2015 Mar 06;6:6453. (PMID: 25743609)
      J Biol Chem. 2016 Sep 9;291(37):19387-400. (PMID: 27445337)
      Protein Sci. 2004 Jun;13(6):1603-11. (PMID: 15133158)
      Mol Cell. 2006 Jun 9;22(5):701-7. (PMID: 16762842)
      Elife. 2017 Mar 21;6:. (PMID: 28323618)
      Structure. 2014 May 6;22(5):707-18. (PMID: 24657090)
      Microbiol Mol Biol Rev. 2007 Mar;71(1):158-229. (PMID: 17347522)
      Mol Microbiol. 2015 Oct;98(1):175-92. (PMID: 26135212)
      PLoS Genet. 2012;8(8):e1002877. (PMID: 22912595)
      FEBS Lett. 2012 Jan 20;586(2):132-6. (PMID: 22200572)
      Nucleic Acids Res. 2006;34(21):6074-82. (PMID: 17099236)
      EMBO J. 1990 May;9(5):1383-9. (PMID: 1691706)
      Curr Protoc Mol Biol. 2007 Apr;Chapter 1:Unit 1.16. (PMID: 18265390)
      Science. 2005 Aug 19;309(5738):1245-8. (PMID: 16109881)
      Mol Cell. 2003 Oct;12(4):903-11. (PMID: 14580341)
      Mol Microbiol. 2014 May;92(3):529-42. (PMID: 24589350)
      PLoS Genet. 2011 Aug;7(8):e1002217. (PMID: 21829394)
      Acta Crystallogr D Biol Crystallogr. 2006 Sep;62(Pt 9):1002-11. (PMID: 16929101)
      Proc Natl Acad Sci U S A. 2016 Aug 30;113(35):9792-7. (PMID: 27531961)
      Cell Host Microbe. 2010 Jan 21;7(1):25-37. (PMID: 20114026)
      Annu Rev Microbiol. 2012;66:103-23. (PMID: 22994490)
      Acta Crystallogr D Biol Crystallogr. 2006 Aug;62(Pt 8):859-66. (PMID: 16855301)
      Acta Crystallogr D Biol Crystallogr. 2004 Dec;60(Pt 12 Pt 1):2126-32. (PMID: 15572765)
      Nucleic Acids Res. 2017 Sep 29;45(17):10306-10320. (PMID: 28973472)
      PLoS One. 2013;8(2):e57609. (PMID: 23469034)
      Acta Crystallogr D Biol Crystallogr. 2010 Feb;66(Pt 2):213-21. (PMID: 20124702)
      Biochemistry. 2015 Dec 1;54(47):7048-57. (PMID: 26535789)
      J Biol Chem. 2006 Nov 10;281(45):34258-68. (PMID: 16968693)
      Nucleic Acids Res. 2016 Nov 16;44(20):9860-9871. (PMID: 27599842)
      Nat Microbiol. 2016 Oct 10;2:16183. (PMID: 27723728)
      J Biol Chem. 2014 Jun 20;289(25):17872-84. (PMID: 24794869)
      Nature. 2013 Aug 15;500(7462):350-353. (PMID: 23925114)
      EMBO J. 2004 Apr 7;23(7):1474-82. (PMID: 15014439)
      Proc Natl Acad Sci U S A. 2000 Jul 18;97(15):8278-83. (PMID: 10880568)
      Nature. 2010 Nov 18;468(7322):439-42. (PMID: 21085179)
      J Struct Funct Genomics. 2013 Dec;14(4):135-44. (PMID: 24057978)
      Proc Natl Acad Sci U S A. 2015 Sep 8;112(36):11341-6. (PMID: 26305955)
      Nat Commun. 2015 Jul 09;6:7480. (PMID: 26158745)
      BMC Genomics. 2013 Sep 14;14:622. (PMID: 24034852)
      Mol Biol Evol. 1993 Nov;10(6):1380-95. (PMID: 8277860)
      Acta Crystallogr D Biol Crystallogr. 2003 Jul;59(Pt 7):1124-30. (PMID: 12832754)
      J Bacteriol. 2009 Mar;191(6):1777-86. (PMID: 19124575)
      Curr Opin Microbiol. 2010 Dec;13(6):781-5. (PMID: 21041110)
      Acta Crystallogr A. 2008 Jan;64(Pt 1):112-22. (PMID: 18156677)
      PLoS Pathog. 2015 Jan 08;11(1):e1004592. (PMID: 25569427)
      Mol Biol Evol. 1993 Sep;10(5):1048-59. (PMID: 8412648)
      J Mol Biol. 2015 Nov 20;427(23):3754-65. (PMID: 26388411)
      J Biol Chem. 1994 Sep 30;269(39):24304-9. (PMID: 7929087)
      Cell. 2009 Dec 11;139(6):1084-95. (PMID: 20005802)
      Proc Natl Acad Sci U S A. 2017 Mar 7;114(10):E1951-E1957. (PMID: 28223500)
      Proc Natl Acad Sci U S A. 2010 Nov 9;107(45):19520-4. (PMID: 20974937)
    • Grant Information:
      R01 GM117373 United States GM NIGMS NIH HHS; R24 GM115586 United States GM NIGMS NIH HHS; U01 GM102318 United States GM NIGMS NIH HHS; U54 GM094585 United States GM NIGMS NIH HHS
    • Contributed Indexing:
      Keywords: bacterial competition; toxin-antitoxin systems; two-partner secretion; type V secretion system
    • Accession Number:
      0 (Bacterial Proteins)
      0 (Bacterial Toxins)
      0 (CdiA protein, E coli)
      0 (CdiB protein, E coli)
      0 (Colicins)
      0 (Escherichia coli Proteins)
      0 (Membrane Proteins)
      0 (RelE protein, E coli)
      9014-25-9 (RNA, Transfer)
      EC 3.1.- (Ribonucleases)
      EC 3.1.27.- (Bacillus amyloliquefaciens ribonuclease)
    • Publication Date:
      Date Created: 20190914 Date Completed: 20200623 Latest Revision: 20201105
    • Publication Date:
      20240829
    • Accession Number:
      PMC6834915
    • Accession Number:
      10.1016/j.str.2019.08.010
    • Accession Number:
      31515004