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 Citation Map 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 Request Permissions Citing Articles Citing Articles via HighWire Citing Articles via Google Scholar Google Scholar Articles by Datta, A. K. Articles by Niyogi, K. Search for Related Content PubMed PubMed Citation Articles by Datta, A. K. Articles by Niyogi, K. Social Bookmarking                      What's this?

JBC, Vol. 250, Issue 18, 7313-7319, Sep, 1975

A novel oligoribonuclease of Escherichia coli. II. Mechanism of action

A. K. Datta and K. Niyogi

Detailed studies of the mechanism of action of the novel oligoribonuclease of Escherichia coli described in the previous paper (1) led to the following conclusions. 1. The enzyme prefers a free 3'-hydroxyl group for its action. 2. The enzyme attacks the oligoribonucleotide substrate in a sequential manner from the 3' end producing 5'-ribonucleotides. 3. The mode of attack appears to be processive; the enzyme acts by degrading one oligoribonucleotide chain to completion before proceeding to the hydrolysis of another chain. 4. The reaction rate is inversely proportional to the chain length of the substrate; however, the enzyme has a higher affinity for longer chains. 5. The enzyme activity is markedly inhibited by secondary structure; oligoribonucleotides combined with complementary polyribonucleotides are attacked poorly below the melting temperature of the complex and efficiently above the melting temperature. 6. The enzyme is inhibited by 5'-nucleotides of adenine and guanine; those of cytosine and uracil have a much smaller effect. The enzyme is not inhibited by 3'-nucleotides. 7. Studies with dinucleoside monophosphate show highest reaction rates with pyrimidine sequences in the order: CpCgreater than UpUgreater than CpUgreater than UpC. The presence of guanine at the 3' end is strongly inhibitory, and reaction rates are CpGgreater than UpG=ApGgreater than GpG.
CiteULike    Complore    Connotea    Del.icio.us    Digg    Reddit    Technorati    What's this?

This article has been cited by other articles:

				U. Mechold, G. Fang, S. Ngo, V. Ogryzko, and A. Danchin YtqI from Bacillus subtilis has both oligoribonuclease and pAp-phosphatase activity Nucleic Acids Res., July 26, 2007; 35(13): 4552 - 4561. [Abstract] [Full Text] [PDF]

				U. Mechold, V. Ogryzko, S. Ngo, and A. Danchin Oligoribonuclease is a common downstream target of lithium-induced pAp accumulation in Escherichia coli and human cells. Nucleic Acids Res., January 1, 2006; 34(8): 2364 - 2373. [Abstract] [Full Text] [PDF]

				D. Kennell Processing Endoribonucleases and mRNA Degradation in Bacteria J. Bacteriol., September 1, 2002; 184(17): 4645 - 4657. [Full Text] [PDF]

				Y. Ohnishi, Y. Nishiyama, R. Sato, S. Kameyama, and S. Horinouchi An Oligoribonuclease Gene in Streptomyces griseus J. Bacteriol., August 15, 2000; 182(16): 4647 - 4653. [Abstract] [Full Text]

				S. Ghosh and M. P. Deutscher Oligoribonuclease is an essential component of the mRNA decay pathway PNAS, April 13, 1999; 96(8): 4372 - 4377. [Abstract] [Full Text] [PDF]

				X. Zhang, L. Zhu, and M. P. Deutscher Oligoribonuclease Is Encoded by a Highly Conserved Gene in the 3'-5' Exonuclease Superfamily J. Bacteriol., May 15, 1998; 180(10): 2779 - 2781. [Abstract] [Full Text]

				L. H. Nguyen, J. P. Erzberger, J. Root, and D. M. Wilson III The Human Homolog of Escherichia coli Orn Degrades Small Single-stranded RNA and DNA Oligomers J. Biol. Chem., August 18, 2000; 275(34): 25900 - 25906. [Abstract] [Full Text] [PDF]