Skip Navigation

This Article
Right arrow Print PDF (3123K)
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 (37)
Right arrowRequest Permissions
Right arrow Commercial Re-use Guidelines
for Open Access NAR Content
Google Scholar
Right arrow Articles by Williamson, C. L.
Right arrow Articles by Burke, J. M.
Right arrow Search for Related Content
PubMed
Right arrow PubMed Citation
Right arrow Articles by Williamson, C. L.
Right arrow Articles by Burke, J. M.
Social Bookmarking
Add to CiteULike   Add to Connotea   Add to Del.icio.us  
What's this?

Nucleic Acids Research, 1989, Vol. 17, No. 2 675-689
© 1989

MOLECULAR BIOLOGY

Compensatory mutations demonstrate that P8 and P6 are RNA secondary structure elements important for processing of a group I intron

Cynthia L. Williamson2, Niraj M. Desai2 and John M. Burke1,2,*

1Department of Microbiology, University of Vermont Burlington, VT 05405 2Department of Chemistry, Williams College Williamstown, MA 01267, USA

*To whom correspondence should be addressed

Received September 26, 1988. Revised December 15, 1988. Accepted December 15, 1988.

Compensatory mutations have been constructed which demonstrate that P8 and P6. two of nine proposed base-pairing Interactions characteristic of group I introns, exist within the folded structure of the Tetrahymena thermophila rRNA intervening sequence, and that these secondary structure elements are important for splicing in E. coli and self-splicing in vitro. Two-base mutations in the 5' and 3' segments of P8 are predicted to disrupt P8 and a strong splicing-defective phenotype is observed in each case. A compensatory four-base mutation in P8 is predicted to restore pairing, and results in the restoration of splicing activity to nearly wild type levels. Thus, we conclude that P8 exists and is essential for splicing. In contrast to the strong phenotypes generally exhibited by mutations which disrupt RNA secondary structure, a two-base mutation in L8 the loop between P8[5'] and P8[3'], results in only a slight decrease in splicing activity. We also tested P6, a pairing which is proposed to consist of only two base-pairs in this intron. A two-base mutation in P6[3'] reduces splicing activity to a greater extent than does a two-base mutation in P6[5']. Comparison of the activities of these mutants and a compensatory P6 four-base mutant support the existence of P6, and suggest that the P6 pairing may be particularly important in the exon ligation step of splicing.


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
Y. Ikawa, K. Tsuda, S. Matsumura, S. Atsumi, and T. Inoue
Putative intermediary stages for the molecular evolution from a ribozyme to a catalytic RNP
Nucleic Acids Res., March 1, 2003; 31(5): 1488 - 1496.
[Abstract] [Full Text] [PDF]

Home page
 J BiochemHome page
Y. Ikawa and T. Inoue
Designed Structural-Rearrangement of an Active Group I Ribozyme
J. Biochem., February 1, 2003; 133(2): 189 - 195.
[Abstract] [Full Text] [PDF]

Home page
 Nucleic Acids ResHome page
S. Atsumi, Y. Ikawa, H. Shiraishi, and T. Inoue
Selections for constituting new RNA-protein interactions in catalytic RNP
Nucleic Acids Res., January 15, 2003; 31(2): 661 - 669.
[Abstract] [Full Text] [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.