Methionyl-tRNA synthetase from Escherichia coli. Primary structure of the active crystallised tryptic fragment.
Methionyl-tRNA synthetase from Escherichia coli. Primary structure of the active crystallised tryptic fragment.
复制标题
来自大肠杆菌的甲硫氨酰-tRNA 合成酶。
DOI:
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发表时间:
2005
期刊:
影响因子:
--
通讯作者:
C. Bruton
中科院分区:
文献类型:
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作者:
D. Barker;J. Ebel;R. Jakes;C. Bruton
A 3300-base segment of Escherichia coli chromosomal DNA, cloned into pBR322, will complement a methionine auxotroph in which the lesion is a defective methionyl-tRNA synthetase with a much reduced affinity for methionine. Crude extracts of these transformants contain elevated levels of a protein which has a subunit molecular weight of 66 000, methionyl-tRNA synthetase aminoacylation activity in vitro and which cross-reacts with anti-(methionyl-tRNA synthetase) antibodies. This polypeptide is very slightly larger than the well-characterised and crystallised tryptic fragment of methionyl-tRNA synthetase. A DNA sequence of 1750 residues at one end of the cloned insert codes for a non-terminated open reading frame in which we can locate a large number of methionyl-tRNA synthetase tryptic and chymotryptic peptides. We have also sequenced 300 nucleotides upstream of this coding segment where we find a large invert repeat in the putative methionyl-tRNA synthetase promoter region.
DOI:
10.1126/science.7025207
发表时间:
1981
期刊:
Science (New York, N.Y.)
影响因子:
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作者:
Putney,SD;Royal,NJ;NeumandeVegvar,H;Herlihy,WC;Biemann,K;Schimmel,P
通讯作者:
Schimmel,P