Broadening the mission of an RNA enzyme
dc.contributor.author | Marvin, Michael Charles | en_US |
dc.contributor.author | Engelke, David R. | en_US |
dc.date.accessioned | 2010-01-05T15:09:35Z | |
dc.date.available | 2010-03-01T21:10:28Z | en_US |
dc.date.issued | 2009-12-15 | en_US |
dc.identifier.citation | Marvin, Michael C.; Engelke, David R. (2009). "Broadening the mission of an RNA enzyme." Journal of Cellular Biochemistry 108(6): 1244-1251. <http://hdl.handle.net/2027.42/64531> | en_US |
dc.identifier.issn | 0730-2312 | en_US |
dc.identifier.issn | 1097-4644 | en_US |
dc.identifier.uri | https://hdl.handle.net/2027.42/64531 | |
dc.identifier.uri | http://www.ncbi.nlm.nih.gov/sites/entrez?cmd=retrieve&db=pubmed&list_uids=19844921&dopt=citation | en_US |
dc.description.abstract | The “RNA World” hypothesis suggests that life developed from RNA enzymes termed ribozymes, which carry out reactions without assistance from proteins. Ribonuclease (RNase) P is one ribozyme that appears to have adapted these origins to modern cellular life by adding protein to the RNA core in order to broaden the potential functions. This RNA-protein complex plays diverse roles in processing RNA, but its best-understood reaction is pre-tRNA maturation, resulting in mature 5' ends of tRNAs. The core catalytic activity resides in the RNA subunit of almost all RNase P enzymes but broader substrate tolerance is required for recognizing not only the diverse sequences of tRNAs, but also additional cellular RNA substrates. This broader substrate tolerance is provided by the addition of protein to the RNA core and allows RNase P to selectively recognize different RNAs, and possibly ribonucleoprotein (RNP) substrates. Thus, increased protein content correlated with evolution from bacteria to eukaryotes has further enhanced substrate potential enabling the enzyme to function in a complex cellular environment. J. Cell. Biochem. 108: 1244–1251, 2009. © 2009 Wiley-Liss, Inc. | en_US |
dc.format.extent | 362033 bytes | |
dc.format.extent | 3118 bytes | |
dc.format.mimetype | application/pdf | |
dc.format.mimetype | text/plain | |
dc.publisher | Wiley Subscription Services, Inc., A Wiley Company | en_US |
dc.subject.other | Life and Medical Sciences | en_US |
dc.subject.other | Cell & Developmental Biology | en_US |
dc.title | Broadening the mission of an RNA enzyme | en_US |
dc.type | Article | en_US |
dc.rights.robots | IndexNoFollow | en_US |
dc.subject.hlbsecondlevel | Genetics | en_US |
dc.subject.hlbsecondlevel | Molecular, Cellular and Developmental Biology | en_US |
dc.subject.hlbtoplevel | Health Sciences | en_US |
dc.subject.hlbtoplevel | Science | en_US |
dc.description.peerreviewed | Peer Reviewed | en_US |
dc.contributor.affiliationum | Department of Biological Chemistry, University of Michigan School of Medicine, Ann Arbor, Michigan 48109-0606 | en_US |
dc.contributor.affiliationum | Department of Biological Chemistry, University of Michigan School of Medicine, Ann Arbor, Michigan 48109-0606 ; Department of Biological Chemistry, University of Michigan School of Medicine, Ann Arbor, MI 48109-0606. | en_US |
dc.identifier.pmid | 19844921 | en_US |
dc.description.bitstreamurl | http://deepblue.lib.umich.edu/bitstream/2027.42/64531/1/22367_ftp.pdf | |
dc.identifier.doi | 10.1002/jcb.22367 | en_US |
dc.identifier.source | Journal of Cellular Biochemistry | en_US |
dc.owningcollname | Interdisciplinary and Peer-Reviewed |
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