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Electrostatic Interactions Play a Critical Role in Mycobacterium tuberculosis Hsp16.3 Binding of Substrate Proteins

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Abstract

Mycobacterium tuberculosis Hsp16.3, a member of a small heat shock protein family, has chaperone-like activity in vitro and suppresses thermally or chemically induced aggregation of proteins. The nature of the interactions between Hsp16.3 and the denatured substrate proteins was investigated. A dramatic enhancement of chaperone-like activity of Hsp16.3 upon increasing temperature was accompanied by decreased ANS-detectable surface hydrophobicity. Hsp16.3 exhibited significantly enhanced chaperone-like activity after preincubation at 100°C with almost unchanged surface hydrophobicity. The interaction between Hsp16.3 and dithiothreitol-treated insulin B chains was markedly weakened in the presence of NaCl but greatly enhanced by the addition of a low-polarity alcohol, accompanied by significantly increased and decreased surface hydrophobicity, respectively. A working model for Hsp16.3 binding to its substrate proteins is proposed.

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Authors and Affiliations

  1. Department of Biological Science and Biotechnology and State Key Laboratory of Biomembranes and Membrane Biotechnology, Tsinghua University, Beijing, 100084, P. R, China

    Q. Mao, D. Ke & Z. Chang

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  1. Q. Mao
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  2. D. Ke
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  3. Z. Chang
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Mao, Q., Ke, D. & Chang, Z. Electrostatic Interactions Play a Critical Role in Mycobacterium tuberculosis Hsp16.3 Binding of Substrate Proteins. Biochemistry (Moscow) 66, 904–908 (2001). https://doi.org/10.1023/A:1011960904542

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