Linked Life Data

8182055

Source:http://linkedlifedata.com/resource/pubmed/id/8182055

Statements in which the resource exists as a subject.
PredicateObject
rdf:type
lifeskim:mentions
pubmed:issue
20
pubmed:dateCreated
1994-6-16
pubmed:abstractText
Nitrate reductase (NR), the first enzyme in the nitrate assimilation pathway, is regulated post-transcriptionally in response to light and CO2. In spinach, it has been shown that phosphorylation is one mechanism that mediates this regulation. In this paper, the phosphorylation of NR in Arabidopsis is described in both wild-type and NR- mutant plants. A 110-kDa protein radiolabeled in vivo with 32PO4 was immunoprecipitated with anti-NR antibody from extracts of wild-type plants but not of mutant plants in which the NR gene NIA2 had been deleted. Phosphoamino acid and phosphopeptide analysis showed that, as for spinach, NR from Arabidopsis is phosphorylated on serine and produces multiple phosphopeptides upon digestion with CNBr or trypsin. Analysis of three mutants with lesions in the NIA2 NR structural gene showed that one mutant, chl3-1, has a reduced phosphorylation phenotype that is not complemented by a NR deletion mutant. Comparison of the sequences of the wild-type and chl3-1 NIA2 genes revealed a single base mutation changing a glycine codon to an aspartic acid codon. This glycine, at position 308 in the MoCo domain of NR, is completely conserved in all known eukaryotic NR sequences. Thus, glycine 308 is required for normal activity and phosphorylation of NR, and substitution of this residue with aspartic acid disrupts both processes, most likely by altering the conformation of the NR MoCo domain.
pubmed:grant
pubmed:language
eng
pubmed:journal
pubmed:citationSubset
IM
pubmed:chemical
pubmed:status
MEDLINE
pubmed:month
May
pubmed:issn
0021-9258
pubmed:author
pubmed:issnType
Print
pubmed:day
20
pubmed:volume
269
pubmed:geneSymbol
chl3-1
pubmed:owner
NLM
pubmed:authorsComplete
Y
pubmed:pagination
14497-501
pubmed:dateRevised
2007-11-14
pubmed:meshHeading
pubmed:year
1994
pubmed:articleTitle
A glycine to aspartic acid change in the MoCo domain of nitrate reductase reduces both activity and phosphorylation levels in Arabidopsis.
pubmed:affiliation
Department of Biology, University of California, San Diego, La Jolla 92093-0116.
pubmed:publicationType
Journal Article, Comparative Study, Research Support, U.S. Gov't, P.H.S., Research Support, Non-U.S. Gov't