Linked Life Data

7590306

Source:http://linkedlifedata.com/resource/pubmed/id/7590306

Statements in which the resource exists as a subject.
PredicateObject
rdf:type
lifeskim:mentions
pubmed:issue
1
pubmed:dateCreated
1995-12-12
pubmed:databankReference
pubmed:abstractText
The aspartyl-tRNA synthetase (AspRS)-encoding gene from the archaeon, Pyrococcus sp. KOD1 (KOD1), was cloned and sequenced, and expressed in Escherichia coli. The purified AspRS possessed an aminoacyation activity for tRNA extracted from KOD1. Analysis of the deduced amino-acid sequence (438 aa, 50,893 Da) revealed that the AspRS of KOD1 is a chimerical protein of bacteria and eukarya. Regional analysis showed high sequence similarity to higher eukaryotic enzymes in the central and C-terminal regions which are important for catalytic activity of the enzyme. In contrast, the N-terminal portion exhibits bacterial features and does not possess the higher eukaryotic sequence which is involved in high molecular weight (HMW) complex formation. These results suggest that archaeon AspRS has a eukaryotic-type catalytic mechanism without forming the HMW complex. This is the first example which shows that an archaeal protein possesses eukaryotic and bacterial features.
pubmed:language
eng
pubmed:journal
pubmed:citationSubset
IM
pubmed:chemical
pubmed:status
MEDLINE
pubmed:month
Oct
pubmed:issn
0378-1119
pubmed:author
pubmed:issnType
Print
pubmed:day
16
pubmed:volume
164
pubmed:owner
NLM
pubmed:authorsComplete
Y
pubmed:pagination
153-6
pubmed:dateRevised
2006-11-15
pubmed:meshHeading
pubmed:year
1995
pubmed:articleTitle
Aspartyl-tRNA synthetase of the hyperthermophilic archaeon Pyrococcus sp. KOD1 has a chimerical structure of eukaryotic and bacterial enzymes.
pubmed:affiliation
Department of Biotechnology, Faculty of Engineering, Osaka University, Japan.
pubmed:publicationType
Journal Article, Comparative Study