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J. Biol. Chem., Vol. 277, Issue 1, 843-853, January 4, 2002
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,,,
From the Departments of Nuclear DNA helicase II (NDH II), also designated
RNA helicase A, is a multifunctional protein involved in transcription, RNA processing, and transport. Here we report that NDH II binds to
F-actin. NDH II was partially purified from HeLa nuclear extracts by
ion-exchange chromatography on Bio-Rex 70 and DEAE-Sepharose. Upon
gel-filtration chromatography on Sepharose 4B, partially purified NDH
II resolved into two distinct peaks. The first NDH II peak,
corresponding to the void volume of Sepharose 4B, displayed coelution
with an abundant 42-kDa protein that was subsequently identified as
actin. Several nuclear proteins such as RNA polymerase II, the U5 small
nuclear ribonucleoprotein (RNP)-associated WD40 protein, and
heterogeneous nuclear RNPs (hnRNPs) copurified with NDH II. However,
only hnRNPs A1 and C were found together with NDH II and actin polymers
during gel filtration. NDH II and hnRNP C from the HeLa nuclear extract
coeluted with F-actin on Sepharose 4B in an RNase-resistant manner,
whereas hnRNP A1 was nearly completely removed from F-actin-associated
hnRNP complexes following RNA digestion. The association of NDH II and
hnRNP C with F-actin was abolished by gelsolin, an
F-actin-depolymerizing protein that fragments actin polymers into
oligomers or monomers. Furthermore, NDH II co-immunoprecipitated with
F-actin and hnRNP C, respectively. In vitro translated NDH
II coeluted with F-actin on Sepharose 4B, whereas no coelution with
F-actin was observed for in vitro translated hnRNP A1 or
C1. Binding to F-actin requires an intact C terminus of NDH II and most
likely a native protein conformation. Electron microscopy indicated a
close spatial proximity among NDH II, hnRNP C, and F-actin within the
HeLa nucleus. These results suggest an important function of NDH II in
mediating the attachment of hnRNP-mRPP RNP complexes to the
actin nucleoskeleton for RNA processing, transport, or other
actin-related processes.
Biochemistry,
§ Molecular Cytology/Electron Microscopy, and
¶ Molecular Biophysics/NMR Spectroscopy, Institute of Molecular
Biotechnology, D-07745 Jena, Germany
To whom correspondence should be addressed: Dept. of
Biochemistry, Inst. of Molecular Biotechnology, Beutenbergstr. 11, D-07745 Jena, Germany. Tel.: 49-3641-656291; Fax: 49-3641-656288;
E-mail: fgrosse@imb-jena.de.
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