TmcA functions as a lysine 2-hydroxyisobutyryltransferase to regulate transcription
Protein lysine 2-hydroxyisobutyrylation (Khib) has recently been shown to play a critical role in the regulation of cellular processes. However, the mechanism and functional consequence of Khib in prokaryotes remain unclear. Here we report that TmcA, an RNA acetyltransferase, functions as a lysine 2...
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| Veröffentlicht in: | Nature chemical biology 2022-02, Vol.18 (2), p.142-151 |
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| creator | Dong, Hanyang Zhao, Yujie Bi, Changfen Han, Yue Zhang, Jianji Bai, Xue Zhai, Guijin Zhang, Hui Tian, Shanshan Hu, Deqing Xu, Liyan Zhang, Kai |
| description | Protein lysine 2-hydroxyisobutyrylation (Khib) has recently been shown to play a critical role in the regulation of cellular processes. However, the mechanism and functional consequence of Khib in prokaryotes remain unclear. Here we report that TmcA, an RNA acetyltransferase, functions as a lysine 2-hydroxyisobutyryltransferase in the regulation of transcription. We show that TmcA can effectively catalyze Khib both in vitro and intracellularly, and that R502 is a key site for the Khib catalytic activity of TmcA. Using quantitative proteomics, we identified 467 endogenous candidates targeted by TmcA for Khib in
Escherichia coli
. Interestingly, we demonstrate that TmcA can specifically modulate the DNA-binding activity of H-NS, a nucleoid-associated protein, by catalysis of Khib at K121. Furthermore, this TmcA-targeted Khib regulates transcription of acid-resistance genes and enhances
E. coli
survival under acid stress. Our study reveals transcription regulation mediated by TmcA-catalyzed Khib for bacterial acid resistance.
RNA acetyltransferase TmcA functions as a lysine 2-hydroxyisobutyryltransferase to regulate bacterial transcription in response to acid stress in prokaryotes. |
| doi_str_mv | 10.1038/s41589-021-00906-3 |
| format | Article |
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Escherichia coli
. Interestingly, we demonstrate that TmcA can specifically modulate the DNA-binding activity of H-NS, a nucleoid-associated protein, by catalysis of Khib at K121. Furthermore, this TmcA-targeted Khib regulates transcription of acid-resistance genes and enhances
E. coli
survival under acid stress. Our study reveals transcription regulation mediated by TmcA-catalyzed Khib for bacterial acid resistance.
RNA acetyltransferase TmcA functions as a lysine 2-hydroxyisobutyryltransferase to regulate bacterial transcription in response to acid stress in prokaryotes.</description><identifier>ISSN: 1552-4450</identifier><identifier>EISSN: 1552-4469</identifier><identifier>DOI: 10.1038/s41589-021-00906-3</identifier><identifier>PMID: 34903851</identifier><language>eng</language><publisher>New York: Nature Publishing Group US</publisher><subject>631/337/572 ; 631/45/475/2290 ; 631/92/458 ; Acetyltransferase ; Acetyltransferases - genetics ; Acetyltransferases - metabolism ; Acid resistance ; Acids ; Amino Acid Sequence ; Biochemical Engineering ; Biochemistry ; Bioorganic Chemistry ; Catalysis ; Catalytic activity ; Cell Biology ; Chemistry ; Chemistry and Materials Science ; Chemistry/Food Science ; E coli ; Escherichia coli ; Escherichia coli - genetics ; Escherichia coli - metabolism ; Escherichia coli Proteins - genetics ; Escherichia coli Proteins - metabolism ; Fimbriae Proteins - genetics ; Fimbriae Proteins - metabolism ; Gene Expression Regulation, Bacterial - physiology ; Gene Expression Regulation, Enzymologic - physiology ; Gene regulation ; Lysine ; Models, Molecular ; Prokaryotes ; Protein Binding ; Protein Conformation ; Proteins ; Proteomics ; Ribonucleic acid ; RNA ; Stress, Physiological ; Transcription ; Transcription, Genetic ; Transcriptome</subject><ispartof>Nature chemical biology, 2022-02, Vol.18 (2), p.142-151</ispartof><rights>The Author(s), under exclusive licence to Springer Nature America, Inc. 2021</rights><rights>2021. The Author(s), under exclusive licence to Springer Nature America, Inc.</rights><rights>The Author(s), under exclusive licence to Springer Nature America, Inc. 2021.</rights><lds50>peer_reviewed</lds50><woscitedreferencessubscribed>false</woscitedreferencessubscribed><citedby>FETCH-LOGICAL-c375t-e366ee5c1a4cbc2d48783c159f888cd74900c874ad1d4519085495b02dab4f913</citedby><cites>FETCH-LOGICAL-c375t-e366ee5c1a4cbc2d48783c159f888cd74900c874ad1d4519085495b02dab4f913</cites><orcidid>0000-0003-2800-0531</orcidid></display><links><openurl>$$Topenurl_article</openurl><openurlfulltext>$$Topenurlfull_article</openurlfulltext><thumbnail>$$Tsyndetics_thumb_exl</thumbnail><link.rule.ids>314,780,784,27924,27925</link.rule.ids><backlink>$$Uhttps://www.ncbi.nlm.nih.gov/pubmed/34903851$$D View this record in MEDLINE/PubMed$$Hfree_for_read</backlink></links><search><creatorcontrib>Dong, Hanyang</creatorcontrib><creatorcontrib>Zhao, Yujie</creatorcontrib><creatorcontrib>Bi, Changfen</creatorcontrib><creatorcontrib>Han, Yue</creatorcontrib><creatorcontrib>Zhang, Jianji</creatorcontrib><creatorcontrib>Bai, Xue</creatorcontrib><creatorcontrib>Zhai, Guijin</creatorcontrib><creatorcontrib>Zhang, Hui</creatorcontrib><creatorcontrib>Tian, Shanshan</creatorcontrib><creatorcontrib>Hu, Deqing</creatorcontrib><creatorcontrib>Xu, Liyan</creatorcontrib><creatorcontrib>Zhang, Kai</creatorcontrib><title>TmcA functions as a lysine 2-hydroxyisobutyryltransferase to regulate transcription</title><title>Nature chemical biology</title><addtitle>Nat Chem Biol</addtitle><addtitle>Nat Chem Biol</addtitle><description>Protein lysine 2-hydroxyisobutyrylation (Khib) has recently been shown to play a critical role in the regulation of cellular processes. However, the mechanism and functional consequence of Khib in prokaryotes remain unclear. Here we report that TmcA, an RNA acetyltransferase, functions as a lysine 2-hydroxyisobutyryltransferase in the regulation of transcription. We show that TmcA can effectively catalyze Khib both in vitro and intracellularly, and that R502 is a key site for the Khib catalytic activity of TmcA. Using quantitative proteomics, we identified 467 endogenous candidates targeted by TmcA for Khib in
Escherichia coli
. Interestingly, we demonstrate that TmcA can specifically modulate the DNA-binding activity of H-NS, a nucleoid-associated protein, by catalysis of Khib at K121. Furthermore, this TmcA-targeted Khib regulates transcription of acid-resistance genes and enhances
E. coli
survival under acid stress. Our study reveals transcription regulation mediated by TmcA-catalyzed Khib for bacterial acid resistance.
RNA acetyltransferase TmcA functions as a lysine 2-hydroxyisobutyryltransferase to regulate bacterial transcription in response to acid stress in prokaryotes.</description><subject>631/337/572</subject><subject>631/45/475/2290</subject><subject>631/92/458</subject><subject>Acetyltransferase</subject><subject>Acetyltransferases - genetics</subject><subject>Acetyltransferases - metabolism</subject><subject>Acid resistance</subject><subject>Acids</subject><subject>Amino Acid Sequence</subject><subject>Biochemical Engineering</subject><subject>Biochemistry</subject><subject>Bioorganic Chemistry</subject><subject>Catalysis</subject><subject>Catalytic activity</subject><subject>Cell Biology</subject><subject>Chemistry</subject><subject>Chemistry and Materials Science</subject><subject>Chemistry/Food Science</subject><subject>E coli</subject><subject>Escherichia coli</subject><subject>Escherichia coli - genetics</subject><subject>Escherichia coli - metabolism</subject><subject>Escherichia coli Proteins - genetics</subject><subject>Escherichia coli Proteins - metabolism</subject><subject>Fimbriae Proteins - genetics</subject><subject>Fimbriae Proteins - metabolism</subject><subject>Gene Expression Regulation, Bacterial - physiology</subject><subject>Gene Expression Regulation, Enzymologic - physiology</subject><subject>Gene regulation</subject><subject>Lysine</subject><subject>Models, Molecular</subject><subject>Prokaryotes</subject><subject>Protein Binding</subject><subject>Protein Conformation</subject><subject>Proteins</subject><subject>Proteomics</subject><subject>Ribonucleic acid</subject><subject>RNA</subject><subject>Stress, Physiological</subject><subject>Transcription</subject><subject>Transcription, 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Basic</collection><collection>Genetics Abstracts</collection><collection>MEDLINE - Academic</collection><jtitle>Nature chemical biology</jtitle></facets><delivery><delcategory>Remote Search Resource</delcategory><fulltext>fulltext</fulltext></delivery><addata><au>Dong, Hanyang</au><au>Zhao, Yujie</au><au>Bi, Changfen</au><au>Han, Yue</au><au>Zhang, Jianji</au><au>Bai, Xue</au><au>Zhai, Guijin</au><au>Zhang, Hui</au><au>Tian, Shanshan</au><au>Hu, Deqing</au><au>Xu, Liyan</au><au>Zhang, Kai</au><format>journal</format><genre>article</genre><ristype>JOUR</ristype><atitle>TmcA functions as a lysine 2-hydroxyisobutyryltransferase to regulate transcription</atitle><jtitle>Nature chemical biology</jtitle><stitle>Nat Chem Biol</stitle><addtitle>Nat Chem Biol</addtitle><date>2022-02-01</date><risdate>2022</risdate><volume>18</volume><issue>2</issue><spage>142</spage><epage>151</epage><pages>142-151</pages><issn>1552-4450</issn><eissn>1552-4469</eissn><abstract>Protein lysine 2-hydroxyisobutyrylation (Khib) has recently been shown to play a critical role in the regulation of cellular processes. However, the mechanism and functional consequence of Khib in prokaryotes remain unclear. Here we report that TmcA, an RNA acetyltransferase, functions as a lysine 2-hydroxyisobutyryltransferase in the regulation of transcription. We show that TmcA can effectively catalyze Khib both in vitro and intracellularly, and that R502 is a key site for the Khib catalytic activity of TmcA. Using quantitative proteomics, we identified 467 endogenous candidates targeted by TmcA for Khib in
Escherichia coli
. Interestingly, we demonstrate that TmcA can specifically modulate the DNA-binding activity of H-NS, a nucleoid-associated protein, by catalysis of Khib at K121. Furthermore, this TmcA-targeted Khib regulates transcription of acid-resistance genes and enhances
E. coli
survival under acid stress. Our study reveals transcription regulation mediated by TmcA-catalyzed Khib for bacterial acid resistance.
RNA acetyltransferase TmcA functions as a lysine 2-hydroxyisobutyryltransferase to regulate bacterial transcription in response to acid stress in prokaryotes.</abstract><cop>New York</cop><pub>Nature Publishing Group US</pub><pmid>34903851</pmid><doi>10.1038/s41589-021-00906-3</doi><tpages>10</tpages><orcidid>https://orcid.org/0000-0003-2800-0531</orcidid></addata></record> |
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| subjects | 631/337/572 631/45/475/2290 631/92/458 Acetyltransferase Acetyltransferases - genetics Acetyltransferases - metabolism Acid resistance Acids Amino Acid Sequence Biochemical Engineering Biochemistry Bioorganic Chemistry Catalysis Catalytic activity Cell Biology Chemistry Chemistry and Materials Science Chemistry/Food Science E coli Escherichia coli Escherichia coli - genetics Escherichia coli - metabolism Escherichia coli Proteins - genetics Escherichia coli Proteins - metabolism Fimbriae Proteins - genetics Fimbriae Proteins - metabolism Gene Expression Regulation, Bacterial - physiology Gene Expression Regulation, Enzymologic - physiology Gene regulation Lysine Models, Molecular Prokaryotes Protein Binding Protein Conformation Proteins Proteomics Ribonucleic acid RNA Stress, Physiological Transcription Transcription, Genetic Transcriptome |
| title | TmcA functions as a lysine 2-hydroxyisobutyryltransferase to regulate transcription |
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