Skip Navigation

This Article
Right arrow Print PDF (737K)
Right arrow Alert me when this article is cited
Right arrow Alert me if a correction is posted
Services
Right arrow Email this article to a friend
Right arrow Similar articles in this journal
Right arrow Similar articles in PubMed
Right arrow Alert me to new issues of the journal
Right arrow Add to My Personal Archive
Right arrow Download to citation manager
Right arrow Commercial Re-use Guidelines
for Open Access NAR Content
Google Scholar
Right arrow Articles by Job, D.
Right arrow Articles by Teissere, M.
Right arrow Search for Related Content
PubMed
Right arrow PubMed Citation
Right arrow Articles by Job, D.
Right arrow Articles by Teissere, M.
Social Bookmarking
Add to CiteULike   Add to Connotea   Add to Del.icio.us  
What's this?

Nucleic Acids Research, 1984, Vol. 12, No. 7 3303-3320
© 1984

ENZYMOLOGY

Complex RNA chain elongation kinetics by wheat germ RNA polymerase II

Dominique Job, Robert Durand, Claudette Job and Marcel Teissere

Centre de Biochimie et de Biologie Moléculaire, CBM 2, Centre National de la Recherche Scientifique 31, chemin Joseph Aiguier, 13402 Marseille cedex 9, France

Received January 16, 1984. Revised March 19, 1984. Accepted March 19, 1984.

Kinetics of RNA chain elongation catalyzed by wheat germ RNA polymerase II have been studied using various synthetic DNA templates in the presence of excess dinucleotide monophosphate primers. With single- or double-stranded homopolymer templates, the double reciprocal plots l/(velocity) as a function of l/(nucleotide substrate) exhibit positive, negative or no curvature. With poly (dAT) as template, the mechanism of nucleoside monophosphate incorporation into RNA i s not the ping-pong kinetic mechanism which was derived for E.coli RNA polymerase (6). Noncomplementary nucleoside triphosphates inhibit RNA transcription allosterically. Cordycepin triphosphate behaves as ATP, and not only inhibits AMP incorporation but also that of UMP and GMP on appropriate templates. The reason for this complex kinetic behavior i s not yet understood. Possibilities are raised that there are several nucleoside triphosphate binding sites on wheat germ RNA polymerase II, that additional nucleoside triphosphate dependent enzymatic activities are required for reaction to occur or that the Km value for incorporation of a given nucleoside monophosphate into RNA is dependent on the length of the RNA chain and/or the nucleotide sequence surrounding the complementary base on the DNA template.


Add to CiteULike CiteULike   Add to Connotea Connotea   Add to Del.icio.us Del.icio.us    What's this?




Disclaimer:
Please note that abstracts for content published before 1996 were created through digital scanning and may therefore not exactly replicate the text of the original print issues. All efforts have been made to ensure accuracy, but the Publisher will not be held responsible for any remaining inaccuracies. If you require any further clarification, please contact our Customer Services Department.