Source:http://linkedlifedata.com/resource/pubmed/id/16361254
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rdf:type | |
lifeskim:mentions |
umls-concept:C0001721,
umls-concept:C0022702,
umls-concept:C0026882,
umls-concept:C0035542,
umls-concept:C0086418,
umls-concept:C0162807,
umls-concept:C0205145,
umls-concept:C0348011,
umls-concept:C0521451,
umls-concept:C0596311,
umls-concept:C1330957,
umls-concept:C1421312,
umls-concept:C1705822,
umls-concept:C1709694,
umls-concept:C1710236
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pubmed:issue |
7
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pubmed:dateCreated |
2006-2-13
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pubmed:abstractText |
tRNAs are transcribed as precursors with a 5' end leader and a 3' end trailer. The 5' end leader is processed by RNase P, and in most organisms in all three kingdoms, transfer ribonuclease (tRNase) Z can endonucleolytically remove the 3' end trailer. Long ((L)) and short ((S)) forms of the tRNase Z gene are present in the human genome. tRNase Z(L) processes a nuclear-encoded pre-tRNA approximately 1600-fold more efficiently than tRNase Z(S) and is predicted to have a strong mitochondrial transport signal. tRNase Z(L) could, thus, process both nuclear- and mitochondrially encoded pre-tRNAs. More than 150 pathogenesis-associated mutations have been found in the mitochondrial genome, most of them in the 22 mitochondrially encoded tRNAs. All the mutations investigated in human mitochondrial tRNA(Ser(UCN)) affect processing efficiency, and some affect the cleavage site and secondary structure. These changes could affect tRNase Z processing of mutant pre-tRNAs, perhaps contributing to mitochondrial disease.
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pubmed:grant | |
pubmed:language |
eng
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pubmed:journal | |
pubmed:citationSubset |
IM
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pubmed:chemical |
http://linkedlifedata.com/resource/pubmed/chemical/3'-pre-tRNase,
http://linkedlifedata.com/resource/pubmed/chemical/Endoribonucleases,
http://linkedlifedata.com/resource/pubmed/chemical/RNA,
http://linkedlifedata.com/resource/pubmed/chemical/RNA, Transfer, Ser,
http://linkedlifedata.com/resource/pubmed/chemical/RNA, mitochondrial,
http://linkedlifedata.com/resource/pubmed/chemical/RNA Precursors
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pubmed:status |
MEDLINE
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pubmed:month |
Feb
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pubmed:issn |
0021-9258
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pubmed:author | |
pubmed:issnType |
Print
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pubmed:day |
17
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pubmed:volume |
281
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pubmed:owner |
NLM
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pubmed:authorsComplete |
Y
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pubmed:pagination |
3926-35
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pubmed:dateRevised |
2007-11-14
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pubmed:meshHeading |
pubmed-meshheading:16361254-Endoribonucleases,
pubmed-meshheading:16361254-Humans,
pubmed-meshheading:16361254-Kinetics,
pubmed-meshheading:16361254-Mitochondria,
pubmed-meshheading:16361254-Mitochondrial Diseases,
pubmed-meshheading:16361254-Mutation,
pubmed-meshheading:16361254-RNA,
pubmed-meshheading:16361254-RNA, Transfer, Ser,
pubmed-meshheading:16361254-RNA Precursors,
pubmed-meshheading:16361254-Substrate Specificity
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pubmed:year |
2006
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pubmed:articleTitle |
Naturally occurring mutations in human mitochondrial pre-tRNASer(UCN) can affect the transfer ribonuclease Z cleavage site, processing kinetics, and substrate secondary structure.
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pubmed:affiliation |
York College of The City University of New York, Jamaica, 11451, USA.
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pubmed:publicationType |
Journal Article,
Research Support, Non-U.S. Gov't,
Research Support, N.I.H., Extramural
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