Article
Structural and functional defects caused by point mutations in the alpha-crystallin domain of a bacterial alpha-heat shock protein.
Journal of molecular biology - 9 May 2003
Lentze Nicolas, Studer Sonja, Narberhaus Franz
Abstract excerpt
The diverse family of alpha-crystallin-type small heat shock proteins (alpha-Hsps or sHsps) is characterised by a central, moderately conserved alpha-crystallin domain. Oligomerisation followed by dissociation of subparticles is thought to be a prerequisite for chaperone function. We demonstrate that HspH, a bacterial alpha-Hsp from the soybean-symbiont Bradyrhizobium japonicum, assembles into dynamic complexes...
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