Item request has been placed!
×
Item request cannot be made.
×
Processing Request
Bioinformatic and Functional Characterization of Hsp70s in Myxococcus xanthus.
Item request has been placed!
×
Item request cannot be made.
×
Processing Request
- Additional Information
- Source:
Publisher: American Society for Microbiology Country of Publication: United States NLM ID: 101674533 Publication Model: Electronic Cited Medium: Internet ISSN: 2379-5042 (Electronic) Linking ISSN: 23795042 NLM ISO Abbreviation: mSphere Subsets: MEDLINE
- Publication Information:
Original Publication: Washington, DC : American Society for Microbiology, [2015]-
- Subject Terms:
- Abstract:
Hsp70 proteins are among the most ubiquitous chaperones and play important roles in maintaining proteostasis and resisting environmental stress. Multiple copies of Hsp70s are widely present in eukaryotic cells with redundant and divergent functions, but they have been less well investigated in prokaryotes. Myxococcus xanthus DK1622 is annotated as having many hsp70 genes. In this study, we performed a bioinformatic analysis of Hsp70 proteins and investigated the functions of six hsp70 genes in DK1622, including two genes that encode proteins with the conserved PRK00290 domain (MXAN_3192 and MXAN_6671) and four genes that encode proteins with the cl35085 or cd10170 domain. We found that only MXAN_3192 is essential for cell survival and heat shock induction. MXAN_3192, compared with the other hsp70 genes, has a high transcriptional level, far exceeding that of any other hsp70 gene, which, however, is not the reason for its essentiality. Deletion of MXAN_6671 ( sglK ) led to multiple deficiencies in development, social motility, and oxidative resistance, while deletion of each of the other four hsp70 genes decreased sporulation and oxidative resistance. MXAN_3192 or sglK , but not the other genes, restored the growth deficiency of the E. coli dnaK mutant. Our results demonstrated that the PRK00290 proteins play a central role in the complex cellular functions of M. xanthus , while the other diverse Hsp70 superfamily homologues probably evolved as helpers with some unknown specific functions. IMPORTANCE Hsp70 proteins are highly conserved chaperones that occur in all kingdoms of life. Multiple copies of Hsp70s are often present in genome-sequenced prokaryotes, especially taxa with complex life cycles, such as myxobacteria. We investigated the functions of six hsp70 genes in Myxococcus xanthus DK1622 and demonstrated that the two Hsp70 proteins with the PRK00290 domain play a central role in complex cellular functions in M. xanthus , while other Hsp70 proteins probably evolved as helpers with some unknown specific functions.
(Copyright © 2021 Pan et al.)
- References:
J Bacteriol. 1998 Jan;180(2):218-24. (PMID: 9440508)
Nucleic Acids Res. 2004 Jul 1;32(Web Server issue):W327-31. (PMID: 15215404)
Microbiol Rev. 1990 Dec;54(4):473-501. (PMID: 1708086)
Proc Natl Acad Sci U S A. 1993 Apr 15;90(8):3378-82. (PMID: 8475084)
Nucleic Acids Res. 2019 Jul 2;47(W1):W256-W259. (PMID: 30931475)
Elife. 2019 Oct 14;8:. (PMID: 31609203)
Science. 1964 Oct 9;146(3641):243-4. (PMID: 14185314)
Gene. 1996 Dec 12;183(1-2):153-7. (PMID: 8996101)
J Bacteriol. 2001 Nov;183(21):6282-7. (PMID: 11591671)
Cell. 2013 Aug 1;154(3):623-36. (PMID: 23911325)
Nature. 1999 Aug 12;400(6745):693-6. (PMID: 10458167)
PLoS Genet. 2014 Jul 24;10(7):e1004516. (PMID: 25058675)
Biochim Biophys Acta Gene Regul Mech. 2018 Oct;1861(10):928-937. (PMID: 30496038)
Protein Sci. 2007 Sep;16(9):1803-18. (PMID: 17766381)
Science. 1996 Jun 14;272(5268):1606-14. (PMID: 8658133)
Nucleic Acids Res. 2020 Jan 8;48(D1):D265-D268. (PMID: 31777944)
J Biol Chem. 2015 Apr 3;290(14):8849-62. (PMID: 25635056)
Proc Natl Acad Sci U S A. 2009 May 26;106(21):8471-6. (PMID: 19439666)
Curr Genomics. 2008;9(5):338-248. (PMID: 19471609)
J Med Microbiol. 2010 Sep;59(Pt 9):1061-1068. (PMID: 20576751)
Genomics Proteomics Bioinformatics. 2015 Oct;13(5):321-31. (PMID: 26563468)
Microbiology (Reading). 2014 Mar;160(Pt 3):488-495. (PMID: 24425771)
PLoS Genet. 2013;9(2):e1003306. (PMID: 23437010)
Nucleic Acids Res. 2018 Jan 4;46(D1):D851-D860. (PMID: 29112715)
J Bacteriol. 1997 Dec;179(24):7748-58. (PMID: 9401034)
J Bacteriol. 2007 May;189(10):3751-8. (PMID: 17351044)
Biochemistry. 1998 Jun 2;37(22):7929-40. (PMID: 9609686)
Cell Rep. 2012 Mar 29;1(3):251-64. (PMID: 22832197)
Cell Mol Life Sci. 2005 Mar;62(6):670-84. (PMID: 15770419)
Mol Microbiol. 2007 Nov;66(4):840-57. (PMID: 17919282)
Annu Rev Microbiol. 1979;33:595-639. (PMID: 115383)
Cell. 2006 May 5;125(3):443-51. (PMID: 16678092)
PeerJ. 2015 Feb 03;3:e747. (PMID: 25674362)
Proc Natl Acad Sci U S A. 2000 Jun 6;97(12):6640-5. (PMID: 10829079)
J Bacteriol. 2001 Feb;183(4):1320-8. (PMID: 11157945)
Front Microbiol. 2017 Apr 27;8:733. (PMID: 28496436)
FEBS Lett. 2007 Jul 31;581(19):3702-10. (PMID: 17544402)
Front Microbiol. 2020 Jan 14;11:2. (PMID: 32010119)
Microbiol Rev. 1996 Mar;60(1):70-102. (PMID: 8852896)
J Bacteriol. 2010 Apr;192(7):1875-81. (PMID: 20139189)
Science. 2016 Jul 1;353(6294):aac4354. (PMID: 27365453)
Front Microbiol. 2016 May 26;7:781. (PMID: 27303375)
Proc Natl Acad Sci U S A. 2006 Oct 10;103(41):15200-5. (PMID: 17015832)
J Bacteriol. 1995 Jul;177(13):3695-703. (PMID: 7601833)
Proc Natl Acad Sci U S A. 1996 Oct 1;93(20):10632-7. (PMID: 8855230)
Sci Rep. 2015 Mar 20;5:9363. (PMID: 25791537)
Curr Genet. 2019 Jun;65(3):721-727. (PMID: 30666394)
J Bacteriol. 1998 Oct;180(20):5357-68. (PMID: 9765567)
Mol Microbiol. 1995 Nov;18(3):547-58. (PMID: 8748037)
J Bacteriol. 1978 Feb;133(2):763-8. (PMID: 415048)
J Mol Evol. 1994 Jan;38(1):1-17. (PMID: 8151709)
Mol Cell Biol. 1987 Jul;7(7):2568-77. (PMID: 3302682)
Nucleic Acids Res. 2014 Jul;42(Web Server issue):W320-4. (PMID: 24753421)
J Bacteriol. 2007 Aug;189(15):5675-82. (PMID: 17513469)
IUBMB Life. 2001 May;51(5):283-7. (PMID: 11699872)
- Contributed Indexing:
Keywords: DnaK proteins; Hsp70 superfamily; Myxococcus xanthus; social behavior; stress response; transcription
- Accession Number:
0 (Bacterial Proteins)
0 (HSP72 Heat-Shock Proteins)
- Publication Date:
Date Created: 20210520 Date Completed: 20211203 Latest Revision: 20211214
- Publication Date:
20221213
- Accession Number:
PMC8265645
- Accession Number:
10.1128/mSphere.00305-21
- Accession Number:
34011688
No Comments.