Publication Date:
1991-11-08
Description:
Phylogenetic-comparative and mutational analyses were used to elucidate the structure of the catalytically active RNA component of eubacterial ribonuclease P (RNase P). In addition to the refinement and extension of known structural elements, the analyses revealed a long-range interaction that results in a second pseudoknot in the RNA. This feature strongly constrains the three-dimensional structure of RNase P RNA near the active site. Some RNase P RNAs lack this structure but contain a unique, possibly compensating, structural domain. This suggests that different RNA structures located at different positions in the sequence may have equivalent architectural functions in RNase P RNA.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Haas, E S -- Morse, D P -- Brown, J W -- Schmidt, F J -- Pace, N R -- GM34527/GM/NIGMS NIH HHS/ -- New York, N.Y. -- Science. 1991 Nov 8;254(5033):853-6.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Department of Biology, Indiana University, Bloomington 47405.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/1719634" target="_blank"〉PubMed〈/a〉
Keywords:
Bacillus subtilis/enzymology/genetics
;
Base Composition
;
Base Sequence
;
Biological Evolution
;
Endoribonucleases/*genetics
;
Escherichia coli/enzymology/genetics
;
*Escherichia coli Proteins
;
Models, Molecular
;
Molecular Sequence Data
;
Mutagenesis
;
Nucleic Acid Conformation
;
RNA, Bacterial/*genetics
;
RNA, Catalytic/*genetics
;
Ribonuclease P
Print ISSN:
0036-8075
Electronic ISSN:
1095-9203
Topics:
Biology
,
Chemistry and Pharmacology
,
Computer Science
,
Medicine
,
Natural Sciences in General
,
Physics
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