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J. Biol. Chem., Vol. 275, Issue 39, 30378-30386, September 29, 2000
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From the Department of Cell Biology and Anatomy and the
§ Program in Molecular Biology and Biotechnology,
University of North Carolina at Chapel Hill, North Carolina 27599
Nuclear autoantigenic sperm protein (NASP),
initially described as a highly autoimmunogenic testis and
sperm-specific protein, is a histone-binding protein that is a
homologue of the N1/N2 gene expressed in oocytes of Xenopus
laevis. Here, we report a somatic form of NASP (sNASP) present in
all mitotic cells examined, including mouse embryonic cells and several
mouse and human tissue culture cell lines. Affinity chromatography and
histone isolation demonstrate that NASP from myeloma cells is complexed
only with H1, linker histones. Somatic NASP is a shorter version of
testicular NASP (tNASP) with two deletions in the coding region arising
from alternative splicing and differs from tNASP in its 5' untranslated regions. We examined the relationship between NASP mRNA expression and the cell cycle and report that in cultures of synchronized mouse
3T3 cells and HeLa cells sNASP mRNA levels increase during S-phase
and decline in G2, concomitant with histone mRNA
levels. NASP protein levels remain stable in these cells but become
undetectable in confluent cultures of nondividing CV-1 cells and in
nonmitotic cells in various body tissues. Expression of sNASP mRNA
is regulated during the cell cycle and, consistent with a role as a
histone transport protein, NASP mRNA expression parallels histone
mRNA expression.
The nucleotide sequence(s) reported in this paper has been submitted to the GenBankTM/EMBL Data Bank with accession number(s) AF034610 (tNASP), AF095722 (sNASP).
Characterization of the Histone H1-binding Protein, NASP, as
a Cell Cycle-regulated Somatic Protein*
,
*
This research was supported by NICHD, National Institutes of
Health, through Cooperative Agreement U54HD35041 as part of the Specialized Cooperative Centers Program in Reproductive Research.The costs of publication of this
article were defrayed in part by the
payment of page charges. The article
must therefore be hereby marked
"advertisement" in
accordance with 18 U.S.C. Section
1734 solely to indicate this fact.
Present address: Dept. of Immunobiology, Bulgarian Academy of
Sciences, Sofia 1113, Bulgaria.
¶
To whom correspondence should be addressed: Dept. of Cell
Biology and Anatomy, CB #7090, University of North Carolina at Chapel Hill, Chapel Hill, NC 27599-7090. Tel.: 919-966-5698; Fax:
919-966-1856; E-mail: morand@unc.edu.
Copyright © 2000 by The American Society for Biochemistry and Molecular Biology, Inc.
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