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| Content Provider | World Health Organization (WHO)-Global Index Medicus |
|---|---|
| Author | Jose, Leny Ramachandran, Ranjit Bhagavat, Raghu Gomez, Roshna Lawrence Chandran, Aneesh Raghunandanan, Sajith Omkumar, Ramakrishnapillai Vyomakesannair Chandra, Nagasuma Mundayoor, Sathish Kumar, Ramakrishnan Ajay |
| Description | Country affiliation: India Author Affiliation: Jose L ( Mycobacterium Research Group, Tropical Disease Biology Division, Rajiv Gandhi Centre for Biotechnology, Thiruvananthapuram, India.); Ramachandran R ( Mycobacterium Research Group, Tropical Disease Biology Division, Rajiv Gandhi Centre for Biotechnology, Thiruvananthapuram, India.); Bhagavat R ( Bioinformatics Centre, Indian Institute of Science, Bangalore, India.); Gomez RL ( Mycobacterium Research Group, Tropical Disease Biology Division, Rajiv Gandhi Centre for Biotechnology, Thiruvananthapuram, India.); Chandran A ( Mycobacterium Research Group, Tropical Disease Biology Division, Rajiv Gandhi Centre for Biotechnology, Thiruvananthapuram, India.); Raghunandanan S ( Mycobacterium Research Group, Tropical Disease Biology Division, Rajiv Gandhi Centre for Biotechnology, Thiruvananthapuram, India.); Omkumar RV ( Neurobiology Group, Rajiv Gandhi Centre for Biotechnology, Thiruvananthapuram, India.); Chandra N ( Bioinformatics Centre, Indian Institute of Science, Bangalore, India.); Mundayoor S ( Mycobacterium Research Group, Tropical Disease Biology Division, Rajiv Gandhi Centre for Biotechnology, Thiruvananthapuram, India.); Kumar RA ( Mycobacterium Research Group, Tropical Disease Biology Division, Rajiv Gandhi Centre for Biotechnology, Thiruvananthapuram, India.) |
| Abstract | We isolated an 8 kDa mycobacterial hypothetical protein, Rv3423.1, from the chromatin of human macrophages infected with Mycobacterium tuberculosis H37Rv. Bioinformatics predictions followed by in vitro biochemical assays with purified recombinant protein showed that Rv3423.1 is a novel histone acetyltransferase that acetylates histone H3 at the K9/K14 positions. Transient transfection of macrophages containing GFP-tagged histone H1 with RFP-tagged Rv3423.1 revealed that the protein co-localizes with the chromatin in the nucleus. Co-immunoprecipitation assays confirmed that the Rv3423.1-histone interaction is specific. Rv3423.1 protein was detected in the culture filtrate of virulent but not avirulent M. tuberculosis. Infection of macrophages with recombinant Mycobacterium smegmatis constitutively expressing Rv3423.1 resulted in a significant increase in the number of intracellular bacteria. However, the protein did not seem to offer any growth advantage to free-living recombinant M. smegmatis. It is highly likely that, by binding to the host chromatin, this histone acetyltransferase from M. tuberculosis may manipulate the expression of host genes involved in anti-inflammatory responses to evade clearance and to survive in the intracellular environment. |
| File Format | HTM / HTML |
| ISSN | 1742464X |
| Issue Number | 2 |
| Volume Number | 283 |
| e-ISSN | 17424658 |
| Journal | FEBS Journal |
| Language | English |
| Publisher | Wiley (on behalf of the Federation of European Biochemical Societies) |
| Publisher Date | 2016-01-01 |
| Publisher Place | Great Britain (UK) |
| Access Restriction | One Nation One Subscription (ONOS) |
| Subject Keyword | Discipline Biochemistry Bacterial Proteins Genetics Metabolism Histone Acetyltransferases Mycobacterium Tuberculosis Enzymology Acetyl Coenzyme A Chemistry Chromatin Computer Simulation Gene Expression Regulation, Bacterial Histones Humans Macrophages Microbiology Mycobacterium Smegmatis Pathogenicity Nad Protein Conformation Journal Article Research Support, Non-u.s. Gov't |
| Content Type | Text |
| Resource Type | Article |
| Subject | Cell Biology Biochemistry Molecular Biology |
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