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| Predicate | Object |
|---|---|
| rdf:type | |
| lifeskim:mentions | |
| pubmed:issue |
2
|
| pubmed:dateCreated |
1995-12-4
|
| pubmed:databankReference |
http://linkedlifedata.com/resource/pubmed/xref/GENBANK/L44581,
http://linkedlifedata.com/resource/pubmed/xref/GENBANK/L44582,
http://linkedlifedata.com/resource/pubmed/xref/GENBANK/L44583,
http://linkedlifedata.com/resource/pubmed/xref/GENBANK/L44584,
http://linkedlifedata.com/resource/pubmed/xref/GENBANK/L44585
|
| pubmed:abstractText |
To understand the subcellular roles and the regulation of vacuolar H(+)-ATPases, we have begun to identify the genes encoding the major subunits and to determine their patterns of expression in Arabidopsis thaliana. Two distinct cDNAs (AVA-P1 and AVA-P2) and one genomic sequence (AVA-P3) encoding the 16 kDa subunit have been isolated. The 16 kDa proteolipid is a major component of the membrane integral sector that forms the proton conductance pathway and is required for assembly of the V-ATPase complex. Interestingly, the open reading frame of one full-length cDNA (AVA-P1) and a genomic sequence (AVA-P3) encoded an identical polypeptide of 164 amino acids with a molecular mass of 16,570. The deduced amino acid sequences of the two cDNAs were nearly identical (99%) and hydropathy plots suggested a molecule with four membrane-spanning domains characteristic of V-ATPase proteolipids. The three genes differed mainly in their codon usage and in their 3'-untranslated regions. The coding region of the genomic sequence, AVA-P3, was interrupted by two introns located at the codons for Cys-26 and Arg-121. The presence of additional 16 kDa proteolipid genes was suggested from several polymerase chain reaction (PCR)-amplified fragments that differed from one another in the size of the second intron. PCR 1 had an intron of ca. 800 bp and its identity as AVA-P4, a fourth member of the gene family, was confirmed from sequence analyses of an EST cDNA. The mRNAs of three genes (AVA-P1, AVA-P2 and AVA-P3) were detected in Arabidopsis leaf, root, flower and silique; yet expression of AVA-P1 and AVA-P2 was lower in roots. All three genes were expressed in light- or dark-grown seedlings; however mRNA levels of AVA-P2 were enhanced in etiolated plants. Arabidopsis thaliana, therefore, has at least four distinct genes encoding nearly identical 16 kDa proteolipids, and the enhanced expression of AVA-P2 transcript in etiolated seedlings suggests that an increase in V-ATPase could accompany cell expansion.
|
| pubmed:language |
eng
|
| pubmed:journal | |
| pubmed:citationSubset |
IM
|
| pubmed:chemical | |
| pubmed:status |
MEDLINE
|
| pubmed:month |
Oct
|
| pubmed:issn |
0167-4412
|
| pubmed:author | |
| pubmed:issnType |
Print
|
| pubmed:volume |
29
|
| pubmed:owner |
NLM
|
| pubmed:authorsComplete |
Y
|
| pubmed:pagination |
227-44
|
| pubmed:dateRevised |
2006-11-15
|
| pubmed:meshHeading |
pubmed-meshheading:7579175-Adaptation, Biological,
pubmed-meshheading:7579175-Amino Acid Sequence,
pubmed-meshheading:7579175-Arabidopsis,
pubmed-meshheading:7579175-Base Sequence,
pubmed-meshheading:7579175-Blotting, Northern,
pubmed-meshheading:7579175-Blotting, Southern,
pubmed-meshheading:7579175-DNA, Complementary,
pubmed-meshheading:7579175-Gene Expression,
pubmed-meshheading:7579175-Gene Library,
pubmed-meshheading:7579175-Genes, Plant,
pubmed-meshheading:7579175-Genome, Plant,
pubmed-meshheading:7579175-Light,
pubmed-meshheading:7579175-Molecular Sequence Data,
pubmed-meshheading:7579175-Multigene Family,
pubmed-meshheading:7579175-Protein Conformation,
pubmed-meshheading:7579175-Proteolipids,
pubmed-meshheading:7579175-Proton-Translocating ATPases,
pubmed-meshheading:7579175-Restriction Mapping,
pubmed-meshheading:7579175-Sequence Analysis, DNA,
pubmed-meshheading:7579175-Sequence Homology, Amino Acid,
pubmed-meshheading:7579175-Sequence Homology, Nucleic Acid,
pubmed-meshheading:7579175-Species Specificity,
pubmed-meshheading:7579175-Tissue Distribution,
pubmed-meshheading:7579175-Vacuoles
|
| pubmed:year |
1995
|
| pubmed:articleTitle |
Several distinct genes encode nearly identical to 16 kDa proteolipids of the vacuolar H(+)-ATPase from Arabidopsis thaliana.
|
| pubmed:affiliation |
Department of Plant Biology, University of Maryland, College Park 20742, USA.
|
| pubmed:publicationType |
Journal Article,
Comparative Study,
Research Support, U.S. Gov't, Non-P.H.S.,
Research Support, Non-U.S. Gov't
|