Mitochondrial Protein p32 Can Accumulate in the Nucleus

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 extra...

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Bibliographic Details
Published in:Biochemical and biophysical research communications 2001-03, Vol.281 (5), p.1161-1169
Main Authors: Brokstad, Karl Albert, Kalland, Karl-Henning, Russell, W.C., Matthews, David A.
Format: Article
Language:English
Subjects:
actinomycin D (act. D)
Active Transport, Cell Nucleus - drug effects
Animals
Carrier Proteins
Cell Line
Cell Nucleus - metabolism
COS Cells
Dactinomycin - pharmacology
Fatty Acids, Unsaturated - pharmacology
Gene Products, rev - metabolism
Green Fluorescent Proteins
HeLa Cells
Heterogeneous-Nuclear Ribonucleoproteins
Humans
Hyaluronan Receptors
Indicators and Reagents - metabolism
leptomycin B (LMB)
Luminescent Proteins - genetics
Luminescent Proteins - metabolism
Membrane Glycoproteins
Methanol - chemistry
Mitochondria - metabolism
mitochondrial protein
Mitochondrial Proteins
p32
Receptors, Complement - genetics
Receptors, Complement - metabolism
Recombinant Fusion Proteins - metabolism
Ribonucleoproteins - metabolism
Sequence Deletion
splicing associated protein
Tissue Fixation
Transfection
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Summary: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.
ISSN:0006-291X
1090-2104
DOI:10.1006/bbrc.2001.4473