DNA methylation patterns associated with asparagine synthetase expression in asparagine-overproducing and -auxotrophic cells.
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منابع مشابه
Knockdown of Asparagine Synthetase A Renders Trypanosoma brucei Auxotrophic to Asparagine
Asparagine synthetase (AS) catalyzes the ATP-dependent conversion of aspartate into asparagine using ammonia or glutamine as nitrogen source. There are two distinct types of AS, asparagine synthetase A (AS-A), known as strictly ammonia-dependent, and asparagine synthetase B (AS-B), which can use either ammonia or glutamine. The absence of AS-A in humans, and its presence in trypanosomes, sugges...
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The level of asparagine synthetase is low in 10-mm root tips from corn seedings (Zea mays W64 x W182F) but relatively high in mature root sections taken 20 to 35 mm from the tip. When root tips are excised there is a marked increase in asparagine synthetase over a 5-hour period. In mature root sections, on the other hand, the asparagine synthetase activity declines over the same 5-hour period. ...
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Asparagine synthetase cDNAs containing the complete coding region were isolated from a human fibroblast cDNA library. DNA sequence analysis of the clones showed that the message contained one open reading frame encoding a protein of 64,400 Mr, 184 nucleotides of 5' untranslated region, and 120 nucleotides of 3' noncoding sequence. Plasmids containing the asparagine synthetase cDNAs were used in...
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Asparagine is present in the mature leaves of young pea (Pisum sativum cv Little Marvel) seedlings, and is synthesized in detached shoots. This accumulation and synthesis is greatly enhanced by darkening. In detached control shoots, [(14)C]aspartate was metabolized predominantly to organic acids and, as other workers have shown, there was little labeling of asparagine (after 5 hours, 3.1% of me...
متن کاملOrgan and cellular localization of asparagine synthetase in rice plants.
DNA gel blot analysis suggested that asparagine synthetase (AS; EC 6.3.5.4) occurred as a single gene in rice. A fusion protein consisting of 17 kDa tagged-region from pET32a(+) expression plasmid and 42 kDa N-terminal region of rice AS was first expressed in Escherichia coli. The resulting polypeptide was purified and a mono-specific antibody for rice AS was prepared after affinity-purificatio...
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ژورنال
عنوان ژورنال: Molecular and Cellular Biology
سال: 1989
ISSN: 0270-7306,1098-5549
DOI: 10.1128/mcb.9.7.2922