Eukaryotic ribonuclease P: Increased complexity to cope with the nuclear pre-tRNA pathway
dc.contributor.author | Xiao, Shaohua | en_US |
dc.contributor.author | Houser-Scott, Felicia | en_US |
dc.contributor.author | Engelke, David R. | en_US |
dc.date.accessioned | 2006-04-19T13:34:36Z | |
dc.date.available | 2006-04-19T13:34:36Z | |
dc.date.issued | 2001-04 | en_US |
dc.identifier.citation | Xiao, 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.issn | 0021-9541 | en_US |
dc.identifier.issn | 1097-4652 | en_US |
dc.identifier.uri | https://hdl.handle.net/2027.42/34443 | |
dc.identifier.uri | http://www.ncbi.nlm.nih.gov/sites/entrez?cmd=retrieve&db=pubmed&list_uids=11241345&dopt=citation | en_US |
dc.description.abstract | Ribonuclease 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.extent | 208878 bytes | |
dc.format.extent | 3118 bytes | |
dc.format.mimetype | application/pdf | |
dc.format.mimetype | text/plain | |
dc.language.iso | en_US | |
dc.publisher | John Wiley & Sons, Inc. | en_US |
dc.subject.other | Life and Medical Sciences | en_US |
dc.subject.other | Cell & Developmental Biology | en_US |
dc.title | Eukaryotic ribonuclease P: Increased complexity to cope with the nuclear pre-tRNA pathway | en_US |
dc.type | Article | en_US |
dc.rights.robots | IndexNoFollow | en_US |
dc.subject.hlbsecondlevel | Molecular, Cellular and Developmental Biology | en_US |
dc.subject.hlbsecondlevel | Kinesiology and Sports | 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, The University of Michigan Medical School, Ann Arbor, Michigan 48109-0606 USA | en_US |
dc.contributor.affiliationum | Department of Biological Chemistry, The University of Michigan Medical School, Ann Arbor, Michigan 48109-0606 USA | en_US |
dc.contributor.affiliationum | Department 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.pmid | 11241345 | en_US |
dc.description.bitstreamurl | http://deepblue.lib.umich.edu/bitstream/2027.42/34443/1/1055_ftp.pdf | en_US |
dc.identifier.doi | http://dx.doi.org/10.1002/1097-4652(200104)187:1<11::AID-JCP1055>3.0.CO;2-K | en_US |
dc.identifier.source | Journal of Cellular Physiology | en_US |
dc.owningcollname | Interdisciplinary and Peer-Reviewed |
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