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Eukaryotic ribonuclease P: Increased complexity to cope with the nuclear pre-tRNA pathway

dc.contributor.authorXiao, Shaohuaen_US
dc.contributor.authorHouser-Scott, Feliciaen_US
dc.contributor.authorEngelke, David R.en_US
dc.date.accessioned2006-04-19T13:34:36Z
dc.date.available2006-04-19T13:34:36Z
dc.date.issued2001-04en_US
dc.identifier.citationXiao, Shaohua; Houser-Scott, Felicia; Engelke, David R. (2001)."Eukaryotic ribonuclease P: Increased complexity to cope with the nuclear pre-tRNA pathway." Journal of Cellular Physiology 187(1): 11-20. <http://hdl.handle.net/2027.42/34443>en_US
dc.identifier.issn0021-9541en_US
dc.identifier.issn1097-4652en_US
dc.identifier.urihttps://hdl.handle.net/2027.42/34443
dc.identifier.urihttp://www.ncbi.nlm.nih.gov/sites/entrez?cmd=retrieve&db=pubmed&list_uids=11241345&dopt=citationen_US
dc.description.abstractRibonuclease P is an ancient enzyme that cleaves pre-tRNAs to generate mature 5' ends. It contains an essential RNA subunit in Bacteria, Archaea, and Eukarya, but the degree to which the RNA subunit relies on proteins to supplement catalysis is highly variable. The eukaryotic nuclear holoenzyme has recently been found to contain almost twenty times the protein content of the bacterial enzymes, in addition to having split into at least two related enzymes with distinct substrate specificity. In this review, recent progress in understanding the molecular architecture and functions of nuclear forms of RNase P will be considered. J. Cell. Physiol. 187:11–20, 2001. © 2001 Wiley-Liss, Inc.en_US
dc.format.extent208878 bytes
dc.format.extent3118 bytes
dc.format.mimetypeapplication/pdf
dc.format.mimetypetext/plain
dc.language.isoen_US
dc.publisherJohn Wiley & Sons, Inc.en_US
dc.subject.otherLife and Medical Sciencesen_US
dc.subject.otherCell & Developmental Biologyen_US
dc.titleEukaryotic ribonuclease P: Increased complexity to cope with the nuclear pre-tRNA pathwayen_US
dc.typeArticleen_US
dc.rights.robotsIndexNoFollowen_US
dc.subject.hlbsecondlevelMolecular, Cellular and Developmental Biologyen_US
dc.subject.hlbsecondlevelKinesiology and Sportsen_US
dc.subject.hlbtoplevelHealth Sciencesen_US
dc.subject.hlbtoplevelScienceen_US
dc.description.peerreviewedPeer Revieweden_US
dc.contributor.affiliationumDepartment of Biological Chemistry, The University of Michigan Medical School, Ann Arbor, Michigan 48109-0606 USAen_US
dc.contributor.affiliationumDepartment of Biological Chemistry, The University of Michigan Medical School, Ann Arbor, Michigan 48109-0606 USAen_US
dc.contributor.affiliationumDepartment of Biological Chemistry, The University of Michigan Medical School, Ann Arbor, Michigan 48109-0606 USA ; Department of Biological Chemistry, The University of Michigan Medical School, Ann Arbor, Michigan 48109-0606, USA.en_US
dc.identifier.pmid11241345en_US
dc.description.bitstreamurlhttp://deepblue.lib.umich.edu/bitstream/2027.42/34443/1/1055_ftp.pdfen_US
dc.identifier.doihttp://dx.doi.org/10.1002/1097-4652(200104)187:1<11::AID-JCP1055>3.0.CO;2-Ken_US
dc.identifier.sourceJournal of Cellular Physiologyen_US
dc.owningcollnameInterdisciplinary and Peer-Reviewed


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