Abstract
α-Crystallin-type small heat shock proteins (sHsps) are expressed in many bacteria, animals, plants, and archaea. Among mycoplasmas (Mollicutes), predicted sHsp homologues so far were found only in the Acholeplasmataceae family. In this report, we describe the cloning and functional characterization of a novel sHsp orthologue, IbpA protein, present in Acholeplasma laidlawii. Importantly, similar to the endogenously expressed sHsp proteins, the recombinant IbpA protein was able to spontaneously generate oligomers in vitro and to rescue chemically denatured bovine insulin from irreversible denaturation and aggregation. Collectively, these data suggest that IbpA is a bona fide member of the sHsps family. The immuneelectron microscopy data using specific antibodies against IbpA have revealed different intracellular localization of this protein in A. laidlawii cells upon heat shock, which suggests that IbpA not only may participate in the stabilization of individual polypeptides, but may also play a protective role in the maintenance of various cellular structures upon temperature stress. © 2011 The Author(s).
Author supplied keywords
Cite
CITATION STYLE
Vishnyakov, I. E., Levitskii, S. A., Manuvera, V. A., Lazarev, V. N., Ayala, J. A., Ivanov, V. A., … Borchsenius, S. N. (2012). The identification and characterization of IbpA, a novel α-crystallin-type heat shock protein from mycoplasma. Cell Stress and Chaperones, 17(2), 171–180. https://doi.org/10.1007/s12192-011-0297-z
Register to see more suggestions
Mendeley helps you to discover research relevant for your work.