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rdf:type |
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lifeskim:mentions |
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pubmed:issue |
3
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pubmed:dateCreated |
1995-2-27
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pubmed:abstractText |
Purification of the glutamate synthase (GOGAT) enzyme from Saccharomyces cerevisiae showed that it is an oligomeric enzyme composed of three identical 199-kDa subunits. The GOGAT structural gene was isolated by screening a yeast genomic library with a yeast PCR probe. This probe was obtained by amplification with degenerate oligonucleotides designed from conserved regions of known GOGAT genes. The derived amino-terminal sequence of the GOGAT gene was confirmed by direct amino-terminal sequence analysis of the purified protein of 199 kDa. Northern (RNA) analysis allowed the identification of an mRNA of about 7 or 8 kb. An internal fragment of the GOGAT gene was used to obtain null GOGAT mutants completely devoid of GOGAT activity. The results show that S. cerevisiae has a single NADH-GOGAT enzyme, consisting of three 199-kDa monomers, that differs from the one found in prokaryotic microorganisms but is similar to those found in other eukaryotic organisms such as alfalfa.
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pubmed:commentsCorrections |
http://linkedlifedata.com/resource/pubmed/commentcorrection/7836314-1348101,
http://linkedlifedata.com/resource/pubmed/commentcorrection/7836314-14907713,
http://linkedlifedata.com/resource/pubmed/commentcorrection/7836314-1587284,
http://linkedlifedata.com/resource/pubmed/commentcorrection/7836314-16662583,
http://linkedlifedata.com/resource/pubmed/commentcorrection/7836314-16666475,
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http://linkedlifedata.com/resource/pubmed/commentcorrection/7836314-1847390,
http://linkedlifedata.com/resource/pubmed/commentcorrection/7836314-1975578,
http://linkedlifedata.com/resource/pubmed/commentcorrection/7836314-1989968,
http://linkedlifedata.com/resource/pubmed/commentcorrection/7836314-2198943,
http://linkedlifedata.com/resource/pubmed/commentcorrection/7836314-238954,
http://linkedlifedata.com/resource/pubmed/commentcorrection/7836314-241744,
http://linkedlifedata.com/resource/pubmed/commentcorrection/7836314-2643092,
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http://linkedlifedata.com/resource/pubmed/commentcorrection/7836314-2848575,
http://linkedlifedata.com/resource/pubmed/commentcorrection/7836314-2856130,
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http://linkedlifedata.com/resource/pubmed/commentcorrection/7836314-3611052,
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http://linkedlifedata.com/resource/pubmed/commentcorrection/7836314-8219058,
http://linkedlifedata.com/resource/pubmed/commentcorrection/7836314-8286406,
http://linkedlifedata.com/resource/pubmed/commentcorrection/7836314-8428988,
http://linkedlifedata.com/resource/pubmed/commentcorrection/7836314-8453303
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pubmed:language |
eng
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pubmed:journal |
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pubmed:citationSubset |
IM
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pubmed:chemical |
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pubmed:status |
MEDLINE
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pubmed:month |
Feb
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pubmed:issn |
0021-9193
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pubmed:author |
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pubmed:issnType |
Print
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pubmed:volume |
177
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pubmed:owner |
NLM
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pubmed:authorsComplete |
Y
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pubmed:pagination |
792-8
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pubmed:dateRevised |
2010-9-13
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pubmed:meshHeading |
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pubmed:year |
1995
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pubmed:articleTitle |
Saccharomyces cerevisiae has a single glutamate synthase gene coding for a plant-like high-molecular-weight polypeptide.
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pubmed:affiliation |
Dipartimento di Biopatologia Umana Policlinico Umberto I. Universitá di Roma La Sapienza, Italy.
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pubmed:publicationType |
Journal Article,
Research Support, Non-U.S. Gov't
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