Skip Navigation

This Article
Right arrow Print PDF (3887K)
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 Search for citing articles in:
ISI Web of Science (30)
Right arrowRequest Permissions
Right arrow Commercial Re-use Guidelines
for Open Access NAR Content
Google Scholar
Right arrow Articles by Sakamoto, H.
Right arrow Articles by Shimura, Y.
Right arrow Search for Related Content
PubMed
Right arrow PubMed Citation
Right arrow Articles by Sakamoto, H.
Right arrow Articles by Shimura, Y.
Social Bookmarking
 Add to CiteULike   Add to Connotea   Add to Del.icio.us  
What's this?

Nucleic Acids Research, 1983, Vol. 11, No. 23 8237-8251
© 1983


MOLECULAR BIOLOGY

Nucleotide sequence and stability of the RNA component of RNase P from a temperature-sensitive mutant of E. coli

Hiroshi Sakamoto, Naohiro Kimura, Fumikiyo Nagawa* and Yoshiro Shimura

Department of Biophysics, Faculty of Science, Kyoto University Kyoto 606, Japan

Received September 14, 1983. Accepted October 25, 1983.

The gene coding for the RNA component of RNase P was cloned from a temperature-sensitive mutant of Escherichia coli defective in RNase P activity (ts7O9) and its parental wild-type strain (4273), and the complete nucleotide sequences of the gene and its flanking regions were determined. The 5'- and 3'-terminal sequences of the RNA component were determined and mapped on the DNA sequence. The mutant gene has GC-to-AT substitutions at positions corresponding to 89 and 365 nucleotides downstream from the 5' terminus of the RNA sequence. Comparing to the wild-type RNA, the mutant RNA is less stable and rapidly degraded in vivo and in vitro.


*Present address: Central Research Institute, Wakunaga Pharmaeutical Co., Koda-cho, Hiroshima 729-64.


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
Nucleic Acids ResHome page
E. Kikovska, N.-E. Mikkelsen, and L. A. Kirsebom
The naturally trans-acting ribozyme RNase P RNA has leadzyme properties
Nucleic Acids Res., December 6, 2005; 33(21): 6920 - 6930.
[Abstract] [Full Text] [PDF]


Home page
ScienceHome page
D. Waugh, C. Green, and N. Pace
The design and catalytic properties of a simplified ribonuclease P RNA
Science, June 30, 1989; 244(4912): 1569 - 1571.
[Abstract] [PDF]


Home page
ScienceHome page
C Reich, G. Olsen, B Pace, and N. Pace
Role of the protein moiety of ribonuclease P, a ribonucleoprotein enzyme
Science, January 8, 1988; 239(4836): 178 - 181.
[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.