Titel
Independent evolution of the core domain and its flanking sequences in small heat shock proteins
Autor*in
Thomas Kriehuber
Technische Universität München
Autor*in
Thomas Rattei
Autor*in
Thomas Weinmaier
... show all
Abstract
Small heat shock proteins (sHsps) are molecular chaperones involved in maintaining protein homeostasis; they have also been implicated in protein folding diseases and in cancer. In this protein family, a conserved core domain, the so-called a-crystallin or Hsp20 domain, is flanked by highly variable, nonconserved sequences that are essential for chaperone function. Analysis of 8714 sHsps revealed a broad variation of primary sequences within the superfamily as well as phyla-dependent differences. Significant variations were found in the number of sHsps per genome, their amino acid composition, and the length distribution of the different sequence parts. Reconstruction of the evolutionary tree for the sHsp superfamily shows that the flanking regions fall into several subgroups, indicating that they were remodeled several times in parallel but independent of the evolution of the a-crystallin domain. The evolutionary history of sHsps is thus set apart from that of other protein families in that two exon boundary-independent strategies are combined: the evolution of the conserved a-crystallin domain and the independent evolution of the N- and C-terminal sequences. This scenario allows for increased variability in specific small parts of the protein and thus promotes functional and structural differentiation of sHsps, which is not reflected in the general evolutionary tree of species.—Kriehuber, T., Rattei, T., Weinmaier, T., Bepperling, A., Haslbeck, M., Buchner, J. Independent evolution of the core domain and its flanking sequences in small heat shock proteins.
Objekt-Typ
Sprache
Englisch [eng]
Persistent identifier
https://phaidra.univie.ac.at/o:243810
Erschienen in
Titel
The FASEB Journal
Band
24
Ausgabe
10
Seitenanfang
3633
Seitenende
3642
Erscheinungsdatum
01.01.2010
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