|
|
|
|
|
|
|
|
|||||
| Home Help Feedback Subscriptions Archive Search Table of Contents | |||||
Journal of Cell Science, Vol 112, Issue 7 1055-1064, Copyright © 1999 by Company of Biologists
JOURNAL ARTICLES |
S Zhang, C Herrmann and F Grosse
Department of Biochemistry and Department of Electron Microscopy and Molecular Cytology, Institute for Molecular Biotechnology, Beutenbergstrasse 11, D-07745 Jena, Germany.
Nuclear DNA helicase II (NDH II), alternatively named RNA helicase A, seems to function as a pre-mRNA and mRNA binding protein in human cells. Immunofluorescence studies of NDH II gave a highly diffused nucleoplasmic staining that was similar to that of hnRNP A1 but differed from the localization of the RNA splicing factor Sc-35. Upon transcriptional inhibition, NDH II migrated from the nucleus into the cytoplasm. During mitosis, NDH II was released into the cytoplasm during pro- to metaphase, and was gradually recruited back into telophase nuclei. The timing of nuclear import of NDH II at telophase was found to be later than that of hnRNP A1 but paralleled that of Sc-35. At the ultrastructural level, both NDH II and hnRNP A1 were identified within perichromatin ribonucleoparticle fibrils. However, the subnuclear distributions of NDH II and hnRNP A1 were not overlapping. NDH II could be extracted together with poly(A)-containing mRNA from HeLa cell nuclei and, to a much lesser extent, from the cytoplasm. Following transcriptional inhibition, NDH II was preferentially associated with mRNA from the cytosol, which biochemically confirmed the microscopic observations. Although NDH II is mainly a nuclear enzyme, it is apparently not associated with the nuclear matrix, since it could be extracted with 2 M NaCl from DNase I-treated nuclei. Our cellular and biochemical observations strongly suggest that NDH II is a pre-mRNA and mRNA binding protein. Its significant affinity for ssDNA, but not for dsDNA, points to a transient role in DNA binding during the process of transcript formation. According to our model, single-stranded DNA might be necessary to retain NDH II in the nuclear compartment.
This article has been cited by other articles:
|
|
 |
|
  T. Valineva, J. Yang, and O. Silvennoinen Characterization of RNA helicase A as component of STAT6-dependent enhanceosome Nucleic Acids Res., September 1, 2006; 34(14): 3938 - 3946. [Abstract] [Full Text] [PDF]
|
|
|
|
|
|
M.-L. Hung, P. Chao, and K.-Y. Chang dsRBM1 and a proline-rich domain of RNA helicase A can form a composite binder to recognize a specific dsDNA Nucleic Acids Res., October 1, 2003; 31(19): 5741 - 5753. [Abstract] [Full Text] [PDF]
|
|
|
|
 |
|
 L. R. SAUNDERS and G. N. BARBER The dsRNA binding protein family: critical roles, diverse cellular functions FASEB J, June 1, 2003; 17(9): 961 - 983. [Abstract] [Full Text] [PDF]
|
|
|
|
 |
|
 B. Fuchsova, P. Novak, J. Kafkova, and P. Hozak Nuclear DNA helicase II is recruited to IFN-{alpha}-activated transcription sites at PML nuclear bodies J. Cell Biol., August 5, 2002; 158(3): 463 - 473. [Abstract] [Full Text] [PDF]
|
|
|
|
 |
|
 S. Zhang, K. Buder, C. Burkhardt, B. Schlott, M. Gorlach, and F. Grosse Nuclear DNA Helicase II/RNA Helicase A Binds to Filamentous Actin J. Biol. Chem., January 4, 2002; 277(1): 843 - 853. [Abstract] [Full Text]
|
|
|
|
|
|
H. Wodrich, A. Schambach, and H.-G. Krausslich Multiple copies of the Mason-Pfizer monkey virus constitutive RNA transport element lead to enhanced HIV-1 Gag expression in a context-dependent manner Nucleic Acids Res., February 15, 2000; 28(4): 901 - 910. [Abstract] [Full Text] [PDF]
|
|
|
|
 |
|
 S Zhang, C Herrmann, and F Grosse Nucleolar localization of murine nuclear DNA helicase II (RNA helicase A) J. Cell Sci., January 8, 1999; 112(16): 2693 - 2703. [Abstract] [PDF]
|
|
|
|
|
|
H. Tang and F. Wong-Staal Specific Interaction between RNA Helicase A and Tap, Two Cellular Proteins That Bind to the Constitutive Transport Element of Type D Retrovirus J. Biol. Chem., October 13, 2000; 275(42): 32694 - 32700. [Abstract] [Full Text] [PDF]
|
|
