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Significance of the C‐terminal globular domain and the extra tail of the calmodulin‐like protein ( Pinctada fucata ) in subcellular localization and protein—protein interaction
Author(s) -
Fang Zi,
Cao Weizhong,
Li Shuo,
Wang Qin,
Li Changzhong,
Xie Liping,
Zhang Rongqing
Publication year - 2008
Publication title -
cell biology international
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 0.932
H-Index - 77
eISSN - 1095-8355
pISSN - 1065-6995
DOI - 10.1016/j.cellbi.2008.04.007
Subject(s) - cytoplasm , immunoprecipitation , microbiology and biotechnology , biology , confocal microscopy , green fluorescent protein , nucleus , calmodulin , colocalization , biochemistry , gene , enzyme
Calmodulin (CaM) plays a very important role in many physiological processes and is highly conserved in different species. In a previous study, we successfully cloned CaM and a novel calmodulin‐like protein (CaLP) with an extra C‐terminal sequence from the pearl oyster Pinctada fucata and then expressed in Escherichia coli . In this research, we used fluorescence confocal microscopy to analyze the protein—protein interaction between CaM/CaLP and p21 Cip1 , which is cloned from mammalian cells, to show the different characteristics of these two proteins in vivo . The fluorescence confocal microscopy showed that the C‐terminal globular domain together with the extra tail of CaLP is very important in CaLP's sequestration in cytoplasm. The most interesting phenomenon is that transfection of p21 Cip1 can stimulate translocation of CaLP from the cytoplasm to the nucleus, but this is not the case for CaM. Fluorescence confocal microscopy and co‐immunoprecipitation on different mutants of CaLP with p21 Cip1 indicated that the C‐terminal globular domain of CaLP is responsible for the trafficking of CaLP from cytoplasm to nucleus.