In silico identification and biochemical characterization of the human dicarboxylate clamp TPR protein interaction network

Bernadotte, A.; Kumar, R.; Winblad, B.; Pavlov, P.F.

Авторы: Bernadotte Alexandra, Kumar Rajnish, Winblad Bengt, Pavlov Pavel F.
Журнал: FEBS open bio
Том: 8
Номер: 11
Год издания: 2018
Издательство: John Wiley & Sons Inc.
Местоположение издательства: United States
Первая страница: 1830
Последняя страница: 1843
DOI: 10.1002/2211-5463.12521
Аннотация: Dicarboxylate clamp tetratricopeptide repeat (dcTPR) motif-containing proteins are well-known partners of the heat shock protein (Hsp) 70 and Hsp90 molecular chaperones. Together, they facilitate a variety of intracel- lular processes, including protein folding and maturation, protein targeting, and protein degradation. An extreme C-terminal sequence, the EEVD motif, is identical in Hsp70 and Hsp90, and is indispensable for their inter- action with dcTPR proteins. However, almost no information is available on the existence of other potential dcTPR-interacting proteins. We searched the human protein database for proteins with C-terminal sequences similar to that of Hsp70/Hsp90 to identify potential partners of dcTPR proteins. The search identified 112 proteins containing a Hsp70/ Hsp90-like signature at their C termini. Gene Ontology enrichment analysis of identified proteins revealed enrichment of distinct protein classes, such as molecular chaperones and proteins of the ubiquitin–proteasome system, highlighting the possibility of functional specialization of proteins contain- ing a Hsp70/Hsp90-like signature. We confirmed interactions of selected proteins containing Hsp70/Hsp90-like C termini with dcTPR proteins both in vitro and in situ. Analysis of interactions of 10-amino-acid peptides cor- responding to the C termini of identified proteins with dcTPR proteins revealed significant differences in binding strength between various pep- tides. We propose a hierarchical mode of interaction within the dcTPR protein network. These findings describe a novel dcTPR protein interaction networks and provide a rationale for selective regulation of protein–protein interactions within this network.
Добавил в систему: Бернадотт Александра

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In silico identification and biochemical characterization of the human dicarboxylate clamp TPR protein interaction networkстатья

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