Linked Life Data

9484453

Source:http://linkedlifedata.com/resource/pubmed/id/9484453

Statements in which the resource exists as a subject.
PredicateObject
rdf:type
lifeskim:mentions
pubmed:issue
4
pubmed:dateCreated
1998-3-9
pubmed:abstractText
The cyanobacterium Synechocystis 6803 was engineered to produce a D1 protein where one or more of the N-terminal threonines at positions 2, 3 and 4 were replaced by other amino acid residues. No phenotypic effects were found for the T2S or T2L mutations, whereas the T2V, T2L;T4V and T2V;T3V;T4V mutations resulted in reduced photoautotrophic growth rate and oxygen evolving activity. The mutant strain T2V;T3V;T4V exhibited an oxygen evolution activity that was only half of that for the wild-type strain. Despite of that, both accumulation and stability of the D1 protein in the thylakoid membrane appeared unaffected in the mutant.
pubmed:language
eng
pubmed:journal
pubmed:citationSubset
IM
pubmed:chemical
pubmed:status
MEDLINE
pubmed:month
Mar
pubmed:issn
0167-4412
pubmed:author
pubmed:issnType
Print
pubmed:volume
36
pubmed:owner
NLM
pubmed:authorsComplete
Y
pubmed:pagination
585-91
pubmed:dateRevised
2006-11-15
pubmed:meshHeading
pubmed:year
1998
pubmed:articleTitle
Site-specific mutations of the N-terminal threonines in the D1 protein affects photoautotrophic growth but not D1 protein stability in Synechocystis 6803.
pubmed:affiliation
Dept. of Biochemistry, Arrhenius Laboratories, Stockholm University, Sweden.
pubmed:publicationType
Journal Article, Research Support, Non-U.S. Gov't