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Article

Lysine acetylation of Hsp16.3: Effect on its structure, chaperone function and influence towards the growth of Mycobacterium tuberculosis.

International journal of biological macromolecules - 1 May 2024

Barik Subhashree, Panda Alok Kumar, Biswas Viplov Kumar, Das Sheetal, Chakraborty Ayon, Beura Shibangini, Modak Rahul, Raghav Sunil Kumar, Kar Rajiv K, Biswas Ashis

Abstract excerpt

Hsp16.3 plays a vital role in the slow growth of Mycobacterium tuberculosis via its chaperone function. Many secretory proteins, including Hsp16.3 undergo acetylation in vivo. Seven lysine (K) residues (K64, K78, K85, K114, K119, K132 and K136) in Hsp16.3 are acetylated inside pathogen. However, how lysine acetylation affects its structure, chaperone function and pathogen's growth is still elusive. We examined...

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Methodology Data sources Editorial policy Privacy About Contact Helena Bioinformatics

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PMID: 38657928
DOI: 10.1016/j.ijbiomac.2024.131763

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