NapM, a new nucleoid‐associated protein, broadly regulates gene expression and affects mycobacterial resistance to anti‐tuberculosis drugs. Issue 1 (7th May 2016)
- Record Type:
- Journal Article
- Title:
- NapM, a new nucleoid‐associated protein, broadly regulates gene expression and affects mycobacterial resistance to anti‐tuberculosis drugs. Issue 1 (7th May 2016)
- Main Title:
- NapM, a new nucleoid‐associated protein, broadly regulates gene expression and affects mycobacterial resistance to anti‐tuberculosis drugs
- Authors:
- Liu, Yu
Wang, Hongyang
Cui, Tao
Zhou, Xiling
Jia, Yanxia
Zhang, Hua
He, Zheng‐Guo - Abstract:
- Summary: Nucleoid‐associated proteins (NAPs) play important roles in the global organization of bacterial chromosomes. However, potential NAPs and their functions are barely characterized in mycobacteria. In this study, NapM, an alkaline protein, functions as a new NAP. NapM is conserved in all of the sequenced mycobacterial genomes, and can recognize DNA in a length‐dependent but sequence‐independent manner. It prefers AT‐rich DNA and binds to the major groove. NapM possesses a clear DNA‐bridging function, and can protect DNA from DNase I digestion. NapM globally regulates the expression of more than 150 genes and the resistance of Mycobacterium smegmatis to two anti‐tuberculosis drugs, namely, rifampicin and ethambutol. An ABC transporter operon was found to be specifically responsible for the napM ‐dependent ethambutol resistance of M. smegmatis . NapM also presents a similar regulation of anti‐tuberculosis drug resistance in M. tuberculosis . These results suggest that NapM is a new member of the mycobacterial NAP family. Our findings expand the range of identified NAPs and improve the understanding on the relationship between NAPs with antibiotic resistance in mycobacteria. Abstract : NapM represents a new nucleoid‐associated protein and is conserved in all of the sequenced mycobacterial genomes. It recognizes DNA in a length‐dependent but sequence‐independent manner. NapM globally regulates the expression of more than 150 genes and the resistance of MycobacteriumSummary: Nucleoid‐associated proteins (NAPs) play important roles in the global organization of bacterial chromosomes. However, potential NAPs and their functions are barely characterized in mycobacteria. In this study, NapM, an alkaline protein, functions as a new NAP. NapM is conserved in all of the sequenced mycobacterial genomes, and can recognize DNA in a length‐dependent but sequence‐independent manner. It prefers AT‐rich DNA and binds to the major groove. NapM possesses a clear DNA‐bridging function, and can protect DNA from DNase I digestion. NapM globally regulates the expression of more than 150 genes and the resistance of Mycobacterium smegmatis to two anti‐tuberculosis drugs, namely, rifampicin and ethambutol. An ABC transporter operon was found to be specifically responsible for the napM ‐dependent ethambutol resistance of M. smegmatis . NapM also presents a similar regulation of anti‐tuberculosis drug resistance in M. tuberculosis . These results suggest that NapM is a new member of the mycobacterial NAP family. Our findings expand the range of identified NAPs and improve the understanding on the relationship between NAPs with antibiotic resistance in mycobacteria. Abstract : NapM represents a new nucleoid‐associated protein and is conserved in all of the sequenced mycobacterial genomes. It recognizes DNA in a length‐dependent but sequence‐independent manner. NapM globally regulates the expression of more than 150 genes and the resistance of Mycobacterium smegmatis to two anti‐tuberculosis drugs. … (more)
- Is Part Of:
- Molecular microbiology. Volume 101:Issue 1(2016)
- Journal:
- Molecular microbiology
- Issue:
- Volume 101:Issue 1(2016)
- Issue Display:
- Volume 101, Issue 1 (2016)
- Year:
- 2016
- Volume:
- 101
- Issue:
- 1
- Issue Sort Value:
- 2016-0101-0001-0000
- Page Start:
- 167
- Page End:
- 181
- Publication Date:
- 2016-05-07
- Subjects:
- Molecular microbiology -- Periodicals
572.829 - Journal URLs:
- http://www.blackwell-synergy.com/servlet/useragent?func=showIssues&code=mmi&close=2003#C2003 ↗
http://onlinelibrary.wiley.com/journal/10.1111/(ISSN)1365-2958 ↗
http://onlinelibrary.wiley.com/ ↗ - DOI:
- 10.1111/mmi.13383 ↗
- Languages:
- English
- ISSNs:
- 0950-382X
- Deposit Type:
- Legaldeposit
- View Content:
- Available online (eLD content is only available in our Reading Rooms) ↗
- Physical Locations:
- British Library DSC - 5900.817960
British Library DSC - BLDSS-3PM
British Library STI - ELD Digital store - Ingest File:
- 345.xml