A 25-KD INHIBITOR OF ACTIN POLYMERIZATION IS A LOW-MOLECULAR MASS HEAT-SHOCK PROTEIN

被引:398
作者
MIRON, T
VANCOMPERNOLLE, K
VANDEKERCKHOVE, J
WILCHEK, M
GEIGER, B
机构
[1] WEIZMANN INST SCI, DEPT CHEM IMMUNOL, IL-76100 REHOVOT, ISRAEL
[2] STATE UNIV GHENT, GENET LAB, B-9000 GHENT, BELGIUM
关键词
D O I
10.1083/jcb.114.2.255
中图分类号
Q2 [细胞生物学];
学科分类号
071009 ; 090102 ;
摘要
The 25-kD inhibitor of actin polymerization (25-kD IAP), isolated from turkey smooth muscle (Miron, T., M. Wilchek, and B. Geiger. 1988. Eur. J. Biochem. 178:543-553.), is shown here to be a low molecular mass heat shock protein (HSP). Direct sequence analysis of the purified protein, as well as cloning and sequencing of the respective cDNA, disclosed a high degree of homology (67% identity, 80% similarity) to the human 27-kD HSP. Southern blot of chicken genomic DNA disclosed one band, suggesting the presence of a single gene, and Northern blot analysis revealed abundant transcript of approximately 1 kb in gizzard and heart tissues and lower amounts in total 18-d chick embryo RNA and in cultured fibroblasts. Exposure of the latter cells to 45-degrees-C resulted in over 15-fold increase in the apparent level of the 25-kD IAP protein, confirming that its expression is regulated by heat shock. Immunofluorescent microscopic localization indicated that after heat treatment, the levels of the 25-kD IAP were markedly increased and the protein was apparently associated with cytoplasmic granules. Heat shock also had a transient, yet prominent, effect on the microfilament system in cultured fibroblasts: stress fibers disintegrated within 10-15 min after incubation at 45-degrees-C, yet upon further incubation at the elevated temperature, conspicuous actin bundles were apparently reformed.
引用
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页码:255 / 261
页数:7
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