HOME HELP FEEDBACK SUBSCRIPTIONS ARCHIVE SEARCH TABLE OF CONTENTS		QUICK SEARCH:   [advanced] Author: Keyword(s): Year:  Vol:  Page:

This Article Full Text (PDF) Alert me when this article is cited Alert me if a correction is posted Services Email this article to a friend Similar articles in this journal Similar articles in PubMed Alert me to new issues of the journal Download to citation manager Citing Articles Citing Articles via HighWire Citing Articles via Google Scholar Google Scholar Articles by Masutani, C. Articles by Ui, M. Search for Related Content PubMed PubMed Citation Articles by Masutani, C. Articles by Ui, M. Social Bookmarking                      What's this?

J. Biol. Chem., Vol. 265, Issue 18, 10210-10216, Jun, 1990

DNA primase stimulatory factor from mouse FM3A cells has an RNase H activity. Purification of the factor and analysis of the stimulation

C Masutani, T Enomoto, M Suzuki, F Hanaoka and M Ui
Department of Physiological Chemistry, Faculty of Pharmaceutical Sciences, University of Tokyo, Japan.

Two forms of DNA primase stimulatory factor have been purified from mouse FM3A cells and shown to have RNase H activity. One of the factors, which consists of three polypeptides of 42,000, 41,000, and 27,000 daltons, was characterized in its properties as RNase H and DNA primase stimulatory factor. The nucleolytic activity of the factor specifically digested the RNA component of RNA-DNA hybrids in an endonucleolytic manner. The stimulation by the factor was observed in DNA synthesis by DNA primase-DNA polymerase alpha complex on unprimed DNA templates, and the DNA chains synthesized under these conditions in the presence of the factor were much shorter than those synthesized in its absence. The stimulatory effect of the factor on DNA primase activity was directly confirmed with DNA primase dissociated from DNA polymerase alpha by the observation of the increase in the number of synthesized oligoribonucleotides. The primer RNA synthesis by DNA primase-DNA polymerase alpha complex under the condition where DNA synthesis occurred was also significantly stimulated by the factor. Furthermore, under these conditions RNA primers were removed from DNA chains by the RNase H activity of the factor.
CiteULike    Complore    Connotea    Del.icio.us    Digg    Reddit    Technorati    What's this?

This article has been cited by other articles:

				W. F. Lima, J. B. Rose, J. G. Nichols, H. Wu, M. T. Migawa, T. K. Wyrzykiewicz, A. M. Siwkowski, and S. T. Crooke Human RNase H1 Discriminates between Subtle Variations in the Structure of the Heteroduplex Substrate Mol. Pharmacol., January 1, 2007; 71(1): 83 - 91. [Abstract] [Full Text] [PDF]

				H. Wu, W. F. Lima, and S. T. Crooke Properties of Cloned and Expressed Human RNase H1 J. Biol. Chem., October 1, 1999; 274(40): 28270 - 28278. [Abstract] [Full Text] [PDF]

				P. Frank, C. Braunshofer-Reiter, U. Wintersberger, R. Grimm, and W. Busen Cloning of the cDNA encoding the large subunit of human RNase HI, a homologue of the prokaryotic RNase HII PNAS, October 27, 1998; 95(22): 12872 - 12877. [Abstract] [Full Text] [PDF]