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Cell Biol Int. 2013 Apr;37(4):359-69. doi: 10.1002/cbin.10043. Epub 2013 Feb 4.

Polypeptide chain release factor eRF3 is a novel molecular partner of survivin.

Author information

1
Key Laboratory of Chemical Biology and Molecular Engineering, Ministry of Education, China; Institute of Biotechnology, Shanxi University, Taiyuan 030006, China.

Abstract

The eukaryotic class II polypeptide chain release factor (eRF3) is an eRF1- and ribosome-dependent GTPase involved in translation termination of protein biosynthesis. eRF3 is a multifunctional protein that is also involved in chromosomal segregation and cytokinesis during mitosis. Survivin is a member of the inhibitor of apoptosis protein (IAP) family that is involved in the organisation of spindle and cell apoptosis. Interaction between survivin and eRF3a-F3 or eRF3b, encoded by the GSPT1 and GSPT2 genes, respectively, was confirmed using yeast two-hybrid (Y2H) and pull-down assays in vitro, and co-immunoprecipitation in vivo. The domains involved in the formation of the survivin-eRF3s complex have been identified. The sites on survivin that interact with eRF3 are located in the baculovirus IAP repeat domain (residues 65-76), which forms a beta-strand structure with an overall negative charge. The sites on eRF3 that interact with survivin were localised to the N-terminal domain(NTD; residues 131-200). Cell localisation experiments indicate that both factors are in the nucleus, suggesting that they cooperatively function in nuclear processes.

KEYWORDS:

cellular localisation; eRF3; interaction map; survivin

PMID:
23377885
DOI:
10.1002/cbin.10043
[Indexed for MEDLINE]

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