Einzeltreffer — DigiBib

Phage G has the largest capsid and genome of any known propagated phage. Many aspects of its structure, assembly, and replication have not been elucidated. Herein, we present the dsDNA-packed and empty phage G capsid at 6.1 and 9 Å resolution, respectively, using cryo-EM for structure determination and mass spectrometry for protein identification. The major capsid protein, gp27, is identified and found to share the HK97-fold universally conserved in all previously solved dsDNA phages. Trimers of the decoration protein, gp26, sit on the 3-fold axes and are thought to enhance the interactions of the hexameric capsomeres of gp27, for other phages encoding decoration proteins. Phage G's decoration protein is longer than what has been reported in other phages, and we suspect the extra interaction surface area helps stabilize the capsid. We identified several additional capsid proteins, including a candidate for the prohead protease responsible for processing gp27. Furthermore, cryo-EM reveals a range of partially full, condensed DNA densities that appear to have no contact with capsid shell. Three analyses confirm that the phage G host is a Lysinibacillus, and not Bacillus megaterium: identity of host proteins in our mass spectrometry analyses, genome sequence of the phage G host, and host range of phage G.

Titel:	Phage G Structure at 6.1 Å Resolution, Condensed DNA, and Host Identity Revision to a Lysinibacillus.
Autor/in / Beteiligte Person:	González, B ; Monroe, L ; Li, K ; Yan, R ; Wright, E ; Walter, T ; Kihara, D ; Weintraub, ST ; Thomas, JA ; Serwer, P ; Jiang, W
Zeitschrift:	Journal of molecular biology, Jg. 432 (2020-06-26), Heft 14, S. 4139-4153
Veröffentlichung:	Amsterdam : Elsevier ; <i>Original Publication</i>: 1959- : London : Academic Press, 2020
Medientyp:	academicJournal
ISSN:	1089-8638 (electronic)
DOI:	10.1016/j.jmb.2020.05.016
Schlagwort:	Bacteriophages genetics Cryoelectron Microscopy DNA Packaging genetics DNA, Viral genetics Humans Virus Assembly genetics Bacteriophages ultrastructure Capsid Proteins genetics DNA, Viral ultrastructure Nucleic Acid Conformation
Sonstiges:	Nachgewiesen in: MEDLINE Sprachen: English Publication Type: Journal Article; Research Support, N.I.H., Extramural; Research Support, U.S. Gov't, Non-P.H.S. Language: English [J Mol Biol] 2020 Jun 26; Vol. 432 (14), pp. 4139-4153. <i>Date of Electronic Publication: </i>2020 May 23. MeSH Terms: Nucleic Acid Conformation* ; Bacteriophages / ultrastructure ; Capsid Proteins / genetics ; DNA, Viral / *ultrastructure ; Bacteriophages / genetics ; Cryoelectron Microscopy ; DNA Packaging / genetics ; DNA, Viral / genetics ; Humans ; Virus Assembly / genetics References: Bioeng Bugs. 2010 Mar-Apr;1(2):85-91. (PMID: 21326933) ; Protein Sci. 2004 Aug;13(8):2260-9. (PMID: 15273316) ; J Struct Biol. 2017 Feb;197(2):102-113. (PMID: 27444392) ; Methods Mol Biol. 2014;1117:401-43. (PMID: 24357374) ; Cold Spring Harb Symp Quant Biol. 1962;27:1-24. (PMID: 14019094) ; Nature. 2006 Feb 2;439(7076):612-6. (PMID: 16452981) ; Microbiology (Reading). 2006 Feb;152(Pt 2):529-534. (PMID: 16436440) ; J Mol Biol. 1975 Jun 5;94(4):555-65. (PMID: 810596) ; Structure. 2018 Feb 6;26(2):238-248.e3. (PMID: 29290487) ; Biophys J. 2011 May 4;100(9):2209-16. (PMID: 21539789) ; J Virol. 2016 Oct 28;90(22):10284-10298. (PMID: 27605673) ; Nucleic Acids Res. 2004 Jul 1;32(Web Server issue):W526-31. (PMID: 15215442) ; Mol Cell Proteomics. 2010 May;9(5):940-51. (PMID: 20233846) ; Virology. 2014 May;456-457:157-70. (PMID: 24889235) ; J Mol Biol. 2018 Jul 20;430(15):2237-2243. (PMID: 29258817) ; Elife. 2019 Apr 04;8:. (PMID: 30945633) ; J Struct Biol. 2007 Jan;157(1):38-46. (PMID: 16859925) ; Structure. 2005 Mar;13(3):413-21. (PMID: 15766543) ; Mol Microbiol. 2010 Jul;77(2):444-55. (PMID: 20497329) ; Virology. 2014 Jul;460-461:138-46. (PMID: 25010279) ; Bacteriophage. 2016 Nov 4;6(4):e1251381. (PMID: 28090386) ; J Mol Biol. 2008 Dec 31;384(5):1384-99. (PMID: 18952096) ; Nucleic Acids Res. 2013 Apr;41(8):4518-24. (PMID: 23449219) ; Structure. 2018 Jul 3;26(7):936-947.e3. (PMID: 29779790) ; Virology. 2015 May;479-480:487-97. (PMID: 25864106) ; Structure. 2013 Feb 5;21(2):298-305. (PMID: 23394943) ; Structure. 2006 Jun;14(6):1073-82. (PMID: 16730179) ; Structure. 2008 Sep 10;16(9):1292-3. (PMID: 18786391) ; J Mol Biol. 1995 Oct 13;253(1):86-99. (PMID: 7473720) ; Structure. 2008 Jun;16(6):935-43. (PMID: 18547525) ; J Mol Biol. 2011 May 6;408(3):541-54. (PMID: 21276801) ; Cell. 1997 Oct 17;91(2):271-80. (PMID: 9346244) ; J Mol Biol. 1995 Apr 7;247(4):636-47. (PMID: 7723020) ; Proc Natl Acad Sci U S A. 2014 Oct 28;111(43):E4606-14. (PMID: 25313071) ; Protein Sci. 2013 Jun;22(6):865-8. (PMID: 23592445) ; Science. 2000 Sep 22;289(5487):2129-33. (PMID: 11000116) ; mBio. 2017 Oct 17;8(5):. (PMID: 29042498) ; J Bacteriol. 2004 Jul;186(13):4369-75. (PMID: 15205439) ; Science. 2018 Aug 31;361(6405):876-880. (PMID: 30166484) ; Proc Natl Acad Sci U S A. 2000 Jun 20;97(13):7248-53. (PMID: 10840059) ; J Struct Biol. 2019 May 1;206(2):183-192. (PMID: 30872095) ; J Mol Biol. 2013 Aug 9;425(15):2765-81. (PMID: 23688818) ; J Mol Biol. 2005 Sep 9;352(1):117-24. (PMID: 16081102) ; Virology. 2014 May;456-457:171-8. (PMID: 24889236) ; Nat Methods. 2013 Jun;10(6):584-90. (PMID: 23644547) ; J Mol Biol. 1992 Feb 20;223(4):999-1011. (PMID: 1538408) ; J Chem Theory Comput. 2017 Apr 11;13(4):1539-1555. (PMID: 28029797) ; J Struct Biol. 2005 Oct;152(1):36-51. (PMID: 16182563) ; Sci Rep. 2016 Nov 08;6:36667. (PMID: 27824135) ; Methods. 2016 May 1;100:50-60. (PMID: 26804562) ; Virology. 2008 Jul 5;376(2):330-8. (PMID: 18474389) ; Q Rev Biophys. 1978 May;11(2):179-246. (PMID: 353876) ; Biophys J. 1997 Feb;72(2 Pt 1):958-63. (PMID: 9017221) ; Nat Rev Microbiol. 2011 Aug 12;9(9):647-57. (PMID: 21836625) ; Virology. 2007 Nov 25;368(2):405-21. (PMID: 17673272) ; Bioinformatics. 2004 Jun 12;20(9):1466-7. (PMID: 14976030) ; Proc Natl Acad Sci U S A. 2011 Jan 25;108(4):1355-60. (PMID: 21220301) ; Nature. 2020 Feb;578(7795):425-431. (PMID: 32051592) ; Nucleic Acids Res. 2014 Aug;42(14):9096-107. (PMID: 25053840) ; Nucleic Acids Res. 2018 Jan 4;46(D1):D624-D632. (PMID: 29145643) ; Structure. 2008 Sep 10;16(9):1399-406. (PMID: 18786402) ; Acta Crystallogr D Biol Crystallogr. 2012 Apr;68(Pt 4):344-51. (PMID: 22505255) ; Proteomics. 2009 Jun;9(11):3215-9. (PMID: 19526553) Grant Information: R01 GM123055 United States GM NIGMS NIH HHS; S10 RR025111 United States RR NCRR NIH HHS; T32 GM132024 United States GM NIGMS NIH HHS; UA5 GM126533 United States GM NIGMS NIH HHS Contributed Indexing: Keywords: DNA condensates; DNA packaging; Lysinibacillus; decoration proteins; phage G Substance Nomenclature: 0 (Capsid Proteins) ; 0 (DNA, Viral) Entry Date(s): Date Created: 20200527 Date Completed: 20201228 Latest Revision: 20210627 Update Code: 20231215 PubMed Central ID: PMC7316594

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Phage G Structure at 6.1 Å Resolution, Condensed DNA, and Host Identity Revision to a Lysinibacillus.

Phage G Structure at 6.1 Å Resolution, Condensed DNA, and Host Identity Revision to a Lysinibacillus.