Redox biology of Mycobacterium tuberculosis H37Rv: protein-protein interaction between GlgB and WhiB1 involves exchange of thiol-disulfide.
IR@IMTECH: CSIR-Institute of Microbial Technology, Chandigarh
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| Title |
Redox biology of Mycobacterium tuberculosis H37Rv: protein-protein interaction between GlgB and WhiB1 involves exchange of thiol-disulfide.
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| Creator |
Garg, Saurabh K
Alam, Md Suhail Bajpai, Richa Kishan, K V Radha Agrawal, Pushpa |
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| Subject |
QR Microbiology
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| Description |
We conclude that M. tuberculosis GlgB has one intra-molecular disulfide bond which is formed between C193 and C617. WhiB1, a thioredoxin like protein interacts with GlgB and transfers its electrons to the disulfide thus reduces the intra-molecular disulfide bond of GlgB. For the first time, we report that GlgB is one of the in vivo substrate of M. tuberculosis WhiB1.
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| Publisher |
BIomedcentral
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| Date |
2009
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| Type |
Article
PeerReviewed |
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| Format |
application/pdf
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| Identifier |
http://crdd.osdd.net/open/571/1/agrawal09.1.pdf
Garg, Saurabh K and Alam, Md Suhail and Bajpai, Richa and Kishan, K V Radha and Agrawal, Pushpa (2009) Redox biology of Mycobacterium tuberculosis H37Rv: protein-protein interaction between GlgB and WhiB1 involves exchange of thiol-disulfide. BMC biochemistry, 10. p. 1. ISSN 1471-2091 |
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| Relation |
http://www.biomedcentral.com/content/pdf/1471-2091-10-1.pdf
http://crdd.osdd.net/open/571/ |
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