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| Content Provider | World Health Organization (WHO)-Global Index Medicus |
|---|---|
| Author | Green, Cathleen M. Kelley, Danielle S. Stanger, Matthew J. Belfort, Marlene Jayachandran, Pradeepa Piazza, Carol Lyn Topilina, Natalya I. Nayak, Sasmita |
| Description | Author Affiliation: Topilina NI ( Department of Biological Sciences and RNA Institute, University at Albany, Albany, NY 12222); Green CM ( Department of Biological Sciences and RNA Institute, University at Albany, Albany, NY 12222); Jayachandran P ( Department of Biological Sciences and RNA Institute, University at Albany, Albany, NY 12222); Kelley DS ( Department of Biomedical Sciences, University at Albany, Albany, NY 12222); Stanger MJ ( Department of Biological Sciences and RNA Institute, University at Albany, Albany, NY 12222); Piazza CL ( Department of Biological Sciences and RNA Institute, University at Albany, Albany, NY 12222); Nayak S ( School of Biotechnology and Kalinga Institute of Medical Sciences, Kalinga Institute of Industrial Technology University, Bhubaneswar, India 751024.); Belfort M ( Department of Biological Sciences and RNA Institute, University at Albany, Albany, NY 12222); |
| Abstract | Inteins are mobile genetic elements that self-splice at the protein level. Mycobacteria have inteins inserted into several important genes, including those corresponding to the iron-sulfur cluster assembly protein SufB. Curiously, the SufB inteins are found primarily in mycobacterial species that are potential human pathogens. Here we discovered an exceptional sensitivity of Mycobacterium tuberculosis SufB intein splicing to oxidative and nitrosative stresses when expressed in Escherichia coli. This effect results from predisposition of the intein's catalytic cysteine residues to oxidative and nitrosative modifications. Experiments with a fluorescent reporter system revealed that reactive oxygen species and reactive nitrogen species inhibit SufB extein ligation by forcing either precursor accumulation or N-terminal cleavage. We propose that splicing inhibition is an immediate, posttranslational regulatory response that can be either reversible, by inducing precursor accumulation, or irreversible, by inducing N-terminal cleavage, which may potentially channel mycobacteria into dormancy under extreme oxidative and nitrosative stresses. |
| ISSN | 00278424 |
| e-ISSN | 10916490 |
| Journal | Proceedings of the National Academy of Sciences of the United States of America |
| Issue Number | 33 |
| Volume Number | 112 |
| Language | English |
| Publisher | National Academy of Sciences |
| Publisher Date | 2015-08-01 |
| Publisher Place | United States |
| Access Restriction | Open |
| Subject Keyword | Carrier Proteins Genetics Escherichia Coli Proteins Inteins Mycobacterium Tuberculosis Protein Splicing Amino Acid Sequence Metabolism Catalysis Computer Simulation Cysteine Chemistry Escherichia Coli Mass Spectrometry Molecular Sequence Data Nitrogen Oxidative Stress Oxygen Plasmids Protein Binding Protein Processing, Post-Translational Protein Structure, Secondary Protein Structure, Tertiary Sequence Homology, Amino Acid Research Support, N.I.H., Extramural Multidisciplinary |
| Content Type | Text |
| Resource Type | Article |
| Subject | Multidisciplinary |
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