Abstract:
:We present evidence that there are at least three Aspergillus nidulans enzymes which catalyze in vitro the reaction of O-acetylserine (OAS) with sulfide forming cysteine. This activity is shared by cysteine synthase (CS) encoded by the cysB gene, homocysteine synthase encoded by cysD and by at least one more enzyme. Moreover, arginine, histidine or proline starvation leads to derepression of CS activity even in the cysB,cysD double mutant strains, while neither cysB nor cysD gene transcription is derepressed by amino acid starvation. Using a cpcA mutant, we show that starvation-inducible CS activity is under control of cross-pathway regulation. We identify CysF as a putative CS in A. nidulans. However, cysF gene transcription is not elevated by amino acid starvation. Therefore, it seems that there exists yet another enzyme, thus far unidentified, which possesses CS activity. Using mutants impaired during various steps of cysteine synthesis we prove that the cysB-encoded enzyme is the only CS of physiological importance in the studied fungus. Similar results were obtained with Schizosaccharomyces pombe mutant strains impaired in cysteine synthesis, indicating that the presence of multiple enzymes with in vitro CS activity may be a common feature of many fungal species.
journal_name
Res Microbioljournal_title
Research in microbiologyauthors
Brzywczy J,Natorff R,Sieńko M,Paszewski Adoi
10.1016/j.resmic.2007.03.002subject
Has Abstractpub_date
2007-06-01 00:00:00pages
428-36issue
5eissn
0923-2508issn
1769-7123pii
S0923-2508(07)00082-4journal_volume
158pub_type
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journal_title:Research in microbiology
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journal_title:Research in microbiology
pub_type: 杂志文章
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pub_type: 杂志文章
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journal_title:Research in microbiology
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journal_title:Research in microbiology
pub_type: 临床试验,杂志文章,评审
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journal_title:Research in microbiology
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journal_title:Research in microbiology
pub_type: 杂志文章
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journal_title:Research in microbiology
pub_type: 杂志文章
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journal_title:Research in microbiology
pub_type: 杂志文章
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