Open AccessProperties of GST-CALM expressed in E. coli
Author(s) -
Jeong-Ah Kim,
Seong-Ryul Kim,
YongKeun Jung,
SoYoun Woo,
JuYoung Seoh,
Young-Sook Hong,
HyungLae Kim
Publication year - 2000
Publication title -
experimental and molecular medicine
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 2.703
H-Index - 82
eISSN - 2092-6413
pISSN - 1226-3613
DOI - 10.1038/emm.2000.17
Subject(s) - clathrin , clathrin adaptor proteins , microbiology and biotechnology , signal transducing adaptor protein , fusion protein , sh3 domain , biology , vesicle , chemistry , endocytosis , biochemistry , gene , proto oncogene tyrosine protein kinase src , receptor , recombinant dna , signal transduction , membrane
Clathrin-coated vesicles (CCVs) are involved in protein and lipid trafficking between intracellular compartments in eukaryotic cells. CCVs are composed of clathrin and assembly proteins. The clathrin assembly protein lymphoid myeloid leukemia (CALM) gene, encodes a homologoue of the neuronal clathrin assembly protein AP180. In this study, we characterized the properties of the CALM expressed in E. coli. The molecular weight of bacterially expressed GST-CALM fusion protein was approximately 105 kD on SDS-PAGE. The CALM protein could promote clathrin triskelia into clathrin cages and could bind the preformed clathrin cage. However, 33 kD N-terminal domain of CALM could not bind pre-assembled clathrin cages, but assemble clathrin triskelia into clathrin cages. The CALM protein was bound to SH3 domain through N-terminal domain1, in vitro. The CALM protein is proteolyzed by caspase 3, caspase 8 and calpain through C-terminal domain.
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