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rdf:type |
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lifeskim:mentions |
umls-concept:C0001128,
umls-concept:C0150312,
umls-concept:C0230373,
umls-concept:C0439659,
umls-concept:C0439858,
umls-concept:C0443177,
umls-concept:C1335439,
umls-concept:C1514562,
umls-concept:C1880389,
umls-concept:C1883204,
umls-concept:C1883221
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pubmed:dateCreated |
2010-7-16
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pubmed:abstractText |
Almost all known nucleic acid polymerases catalyze 5'-3' polymerization by mediating the attack on an incoming nucleotide 5' triphosphate by the 3'OH from the growing polynucleotide chain in a template dependent or independent manner. The only known exception to this rule is the Thg1 RNA polymerase that catalyzes 3'-5' polymerization in vitro and also in vivo as a part of the maturation process of histidinyl tRNA. While the initial reaction catalyzed by Thg1 has been compared to adenylation catalyzed by the aminoacyl tRNA synthetases, the evolutionary relationships of Thg1 and the actual nature of the polymerase reaction catalyzed by it remain unclear.
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pubmed:commentsCorrections |
http://linkedlifedata.com/resource/pubmed/commentcorrection/20591188-10077608,
http://linkedlifedata.com/resource/pubmed/commentcorrection/20591188-10446225,
http://linkedlifedata.com/resource/pubmed/commentcorrection/20591188-11788711,
http://linkedlifedata.com/resource/pubmed/commentcorrection/20591188-12429060,
http://linkedlifedata.com/resource/pubmed/commentcorrection/20591188-12466548,
http://linkedlifedata.com/resource/pubmed/commentcorrection/20591188-12553882,
http://linkedlifedata.com/resource/pubmed/commentcorrection/20591188-14568537,
http://linkedlifedata.com/resource/pubmed/commentcorrection/20591188-15684411,
http://linkedlifedata.com/resource/pubmed/commentcorrection/20591188-15980461,
http://linkedlifedata.com/resource/pubmed/commentcorrection/20591188-16027112,
http://linkedlifedata.com/resource/pubmed/commentcorrection/20591188-16292354,
http://linkedlifedata.com/resource/pubmed/commentcorrection/20591188-16545108,
http://linkedlifedata.com/resource/pubmed/commentcorrection/20591188-16625026,
http://linkedlifedata.com/resource/pubmed/commentcorrection/20591188-16731615,
http://linkedlifedata.com/resource/pubmed/commentcorrection/20591188-16980588,
http://linkedlifedata.com/resource/pubmed/commentcorrection/20591188-18366186,
http://linkedlifedata.com/resource/pubmed/commentcorrection/20591188-18834537,
http://linkedlifedata.com/resource/pubmed/commentcorrection/20591188-20080734,
http://linkedlifedata.com/resource/pubmed/commentcorrection/20591188-3023854,
http://linkedlifedata.com/resource/pubmed/commentcorrection/20591188-6297798,
http://linkedlifedata.com/resource/pubmed/commentcorrection/20591188-9254694,
http://linkedlifedata.com/resource/pubmed/commentcorrection/20591188-9927721
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pubmed:language |
eng
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pubmed:journal |
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pubmed:citationSubset |
IM
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pubmed:chemical |
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pubmed:status |
MEDLINE
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pubmed:issn |
1745-6150
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pubmed:author |
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pubmed:issnType |
Electronic
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pubmed:volume |
5
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pubmed:owner |
NLM
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pubmed:authorsComplete |
Y
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pubmed:pagination |
43
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pubmed:meshHeading |
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pubmed:year |
2010
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pubmed:articleTitle |
Presence of a classical RRM-fold palm domain in Thg1-type 3'- 5'nucleic acid polymerases and the origin of the GGDEF and CRISPR polymerase domains.
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pubmed:affiliation |
National Center for Biotechnology Information, National Library of Medicine, National Institutes of Health, Bethesda, MD 20894, USA.
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pubmed:publicationType |
Journal Article,
Research Support, N.I.H., Extramural
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