期刊
ARCHIVES OF BIOCHEMISTRY AND BIOPHYSICS
卷 549, 期 -, 页码 32-39出版社
ELSEVIER SCIENCE INC
DOI: 10.1016/j.abb.2014.03.008
关键词
14-3-3 monomer; Small heat shock proteins; bis-ANS fluorescence; Aggregation; Moonlight proteins; Hydrophobicity
资金
- Russian Foundation for Basic Research [14-04-00146-a, 14-0401530-a, 13-04-00015-a]
Members of the 14-3-3 protein family interact with hundreds of different, predominantly phosphorylated, proteins. 14-3-3 dimers are prevalent but exist at the equilibrium with the monomers. Our previous studies using the engineered monomeric 14-3-3 zeta (14-3-3 zeta(m)) showed that 14-3-3 zeta monomer retained binding activity towards selected phosphorylated partners and, in addition, it prevented heat-induced aggregation of myosin subfragment 1. Since the chaperone-like activity of 14-3-3 monomers has been insufficiently studied, here we have analyzed the effect of 14-3-3 zeta(m) on the aggregation of different model proteins. We found that 14-3-3 zeta(m) demonstrated considerable chaperone-like activity by inhibiting the DTT-induced aggregation of insulin and thermally-induced aggregation of alcohol dehydrogenase and phosphorylase kinase. Importantly, the anti-aggregating activity of 14-3-3 zeta(m) was concentration-dependent and overall, was more pronounced than that of its dimeric counterpart. In some cases, the chaperone-like effect of 14-3-3 zeta(m) was comparable, or even higher, than that of the small heat shock proteins, HspB6 and HspB5. We suggest that 14-3-3s not only can bind and regulate the activity of multiple phosphoproteins, but also possess moonlighting chaperone-like activity, which is especially pronounced in the case of monomeric forms of 14-3-3 which can be present under certain stress conditions. (C) 2014 Elsevier Inc. All rights reserved.
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