Switch to
Predicate | Object |
---|---|
rdf:type | |
lifeskim:mentions | |
pubmed:issue |
3
|
pubmed:dateCreated |
1995-10-23
|
pubmed:databankReference | |
pubmed:abstractText |
delta 1-pyrroline-5-carboxylate reductase (P5CR; [L-proline: NAD(P+) 5-oxidoreductase]; EC 1.5.1.2) catalyzes the final step in proline biosynthesis. We have shown that the proline-1 (pro-1) locus of Neurospora crassa encodes P5CR. The pro-1 gene was localized to a 3.2 kb region by complementation of (restoration of proline-independent growth to) a proline auxotroph carrying a recessive mutation at the pro-1 locus. The nucleotide sequence of this 3.2 kb region contains an open reading frame with coding capacity of 311 amino acids. The deduced polypeptide shows significant similarity to P5CR amino acid sequences. Similarity of N. crassa P5CR is greatest to that of the yeast, Saccharomyces cerevisiae, but is also strong to P5CR sequences from archaea, eubacteria, plants, and humans. In N. crassa, amino acid imbalance, including deficiency or excess of a single amino acid, such as histidine, induces expression of many amino acid biosynthetic genes that are under cross-pathway control, a general regulatory system analogous to general amino acid control in Saccharomyces. Although P5CR catalyzes the only committed step in proline biosynthesis, pro-1 expression was unaltered by histidine starvation and independent of CPC1, a positively acting transcription factor that mediates cross-pathway control in N. crassa.
|
pubmed:language |
eng
|
pubmed:journal | |
pubmed:citationSubset |
IM
|
pubmed:chemical |
http://linkedlifedata.com/resource/pubmed/chemical/DNA, Fungal,
http://linkedlifedata.com/resource/pubmed/chemical/Membrane Proteins,
http://linkedlifedata.com/resource/pubmed/chemical/Monosaccharide Transport Proteins,
http://linkedlifedata.com/resource/pubmed/chemical/Protozoan Proteins,
http://linkedlifedata.com/resource/pubmed/chemical/Pyrroline Carboxylate Reductases,
http://linkedlifedata.com/resource/pubmed/chemical/delta-1-pyrroline-5-carboxylate...
|
pubmed:status |
MEDLINE
|
pubmed:month |
Aug
|
pubmed:issn |
0026-8925
|
pubmed:author | |
pubmed:issnType |
Print
|
pubmed:day |
21
|
pubmed:volume |
248
|
pubmed:geneSymbol |
pro-1<up>+</up>,
pro-1<up>-</up>
|
pubmed:owner |
NLM
|
pubmed:authorsComplete |
Y
|
pubmed:pagination |
341-50
|
pubmed:dateRevised |
2006-11-15
|
pubmed:meshHeading |
pubmed-meshheading:7565596-Alleles,
pubmed-meshheading:7565596-Amino Acid Sequence,
pubmed-meshheading:7565596-Base Sequence,
pubmed-meshheading:7565596-DNA, Fungal,
pubmed-meshheading:7565596-Gene Expression Regulation, Fungal,
pubmed-meshheading:7565596-Humans,
pubmed-meshheading:7565596-Membrane Proteins,
pubmed-meshheading:7565596-Molecular Sequence Data,
pubmed-meshheading:7565596-Monosaccharide Transport Proteins,
pubmed-meshheading:7565596-Neurospora crassa,
pubmed-meshheading:7565596-Phylogeny,
pubmed-meshheading:7565596-Protozoan Proteins,
pubmed-meshheading:7565596-Pyrroline Carboxylate Reductases,
pubmed-meshheading:7565596-Sequence Homology, Amino Acid,
pubmed-meshheading:7565596-Transcription, Genetic
|
pubmed:year |
1995
|
pubmed:articleTitle |
Molecular characterization of the proline-1 (pro-1) locus of Neurospora crassa, which encodes delta 1-pyrroline-5-carboxylate reductase.
|
pubmed:affiliation |
Department of Biological Sciences, Dartmouth College, Hanover, New Hampshire 03755, USA.
|
pubmed:publicationType |
Journal Article,
Research Support, U.S. Gov't, Non-P.H.S.,
Research Support, Non-U.S. Gov't
|