Skip Navigation

This Article
Right arrow Print PDF (1239K)
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 arrowRequest Permissions
Right arrow Commercial Re-use Guidelines
for Open Access NAR Content
Google Scholar
Right arrow Articles by Minks, M. A.
Right arrow Articles by Baglioni, C.
Right arrow Search for Related Content
PubMed
Right arrow PubMed Citation
Right arrow Articles by Minks, M. A.
Right arrow Articles by Baglioni, C.
Social Bookmarking
Add to CiteULike   Add to Connotea   Add to Del.icio.us  
What's this?

Nucleic Acids Research, 1979, Vol. 6, No. 2 767-780
© 1979

Articles

Metabolic stability of 2' 5'oligo (A) and activity of 2' 5'oligo (A)-dependent endonuclease in extracts of interferon-treated and control HeLa cells

Michael A. Minks, Susan Benvin, Patricia A. Maroney and Corrado Baglioni

Department of Biological Sciences, State University of New York at Albany, Albany NY 12222, USA

Received October 23, 1978. Extracts of interferon-treated HeLa cells adsorbed to poly(I) • poly(C)-agarose have been used to synthesize 2'5'oligo(A). This oligonucleotide has been characterized by enzymatic digestion with alkaline phosphatase, snake venom phosphodiesterase, T2 ribonuclease and chromatography on DEAE, and PEI-cellulose. The oligonucleotide inhibits protein synthesis in vitro and activates an endonuclease present in extracts of control and interferon-treated cells. The metabolic stability of 2'5'oligo(A) has been investigated in these cell extracts. The oligonucleotide undergoes rapid degradation, particularly in the absence of ATP and of an energy regenerating system. Furthermore, the 2'5'oligo(A)-activated endonuclease reverts to an inactive state under these conditions, but can be reactivated upon further addition of 2'5'oligo(A). A possible role for the degradation of 2'5'oligo(A) in the mechanism of interferon action is discussed.


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


This article has been cited by other articles:


Home page
 J. Biol. Chem.Home page
K. Kubota, K. Nakahara, T. Ohtsuka, S. Yoshida, J. Kawaguchi, Y. Fujita, Y. Ozeki, A. Hara, C. Yoshimura, H. Furukawa, et al.
Identification of 2'-Phosphodiesterase, Which Plays a Role in the 2-5A System Regulated by Interferon
J. Biol. Chem., September 3, 2004; 279(36): 37832 - 37841.
[Abstract] [Full Text] [PDF]

Home page
 ScienceHome page
B Ruskin and M. Green
An RNA processing activity that debranches RNA lariats
Science, July 12, 1985; 229(4709): 135 - 140.
[Abstract] [PDF]


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.