Mitochondrial protein p32 can accumulate in the nucleus

被引:54
作者
Brokstad, KA
Kalland, KH
Russell, WC
Matthews, DA
机构
[1] St James Univ Hosp, Mol Med Unit, Leeds LS9 7TF, W Yorkshire, England
[2] Univ Bergen, Broegelmann Res Lab, N-5021 Bergen, Norway
[3] Univ Bergen, Gade Inst, Ctr Virol, Dept Microbiol & Immunol, N-5020 Bergen, Norway
[4] Univ St Andrews, St Andrews KY16 9ST, Fife, Scotland
基金
英国医学研究理事会;
关键词
p32; splicing associated protein; mitochondrial protein; actinomycin D (act. D); leptomycin B (LMB);
D O I
10.1006/bbrc.2001.4473
中图分类号
Q5 [生物化学]; Q7 [分子生物学];
学科分类号
071010 ; 081704 ;
摘要
Human p32 was first isolated associated with the splicing factor ASF/SF-2, The p32 protein is translated as pre-protein from which a mitochondrial import signal is cleaved off to create the mature p32. The majority of p32 is consequently found in the mitochondria. In this study we investigated extramitochondrial p32. An increased nuclear localisation of endogenous p32 was demonstrated as a response to leptomycin B or actinomycin D treatment of cells. Mature p32 gene and deletion mutants were cloned into enhanced green fluorescence protein reporter plasmids. On transfection, EGFP-p32 protein was mainly localised to the cytoplasm and to a lesser extent to the nucleus of transfected COS cells. Upon treatment with actinomycin D or leptomycin B, the EGFP-p32 protein accumulated in the nucleus. Deletion analysis indicated which regions of EGFP-p32 are involved in nuclear export and nuclear import. (C) 2001 Academic Press.
引用
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页码:1161 / 1169
页数:9
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