大肠杆菌甲硫氨酰 - 转运RNA合成酶突变体回复株中依赖rel的甲硫氨酸需求 - Suppr

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超能文献

rel-dependent methionine requirement in revertants of a methionyl-transfer RNA synthetase mutant of Escherichia coli.

作者信息

Somerville C R, Ahmed A

出版信息

J Mol Biol. 1977 Mar 25;111(1):77-81. doi: 10.1016/s0022-2836(77)80133-2.

DOI:10.1016/s0022-2836(77)80133-2

PMID:323499

Abstract

摘要

相似文献

rel-dependent methionine requirement in revertants of a methionyl-transfer RNA synthetase mutant of Escherichia coli.大肠杆菌甲硫氨酰 - 转运RNA合成酶突变体回复株中依赖rel的甲硫氨酸需求

J Mol Biol. 1977 Mar 25;111(1):77-81. doi: 10.1016/s0022-2836(77)80133-2.

A new method for the isolation of methionyl transfer RNA synthetase mutants from Escherichia coli.一种从大肠杆菌中分离甲硫氨酰转移核糖核酸合成酶突变体的新方法。

Can J Microbiol. 1975 Jun;21(6):754-8. doi: 10.1139/m75-112.

The recognition of methionine analogues by Escherichia coli methionyl-transfer ribonucleic acid synthetase.大肠杆菌甲硫氨酰 - 转移核糖核酸合成酶对甲硫氨酸类似物的识别。

Biochem Soc Trans. 1975;3(5):659-60. doi: 10.1042/bst0030659.

Antico-operative binding of bacterial and mammalian initiator tRNAMet to methionyl-tRNA synthetase from escherichia coli.细菌和哺乳动物起始甲硫氨酸转运核糖核酸（tRNAMet）与大肠杆菌甲硫氨酰-tRNA合成酶的抗协同结合

J Mol Biol. 1976 Jun 5;103(4):765-84. doi: 10.1016/0022-2836(76)90208-4.

The aminoacylation of transfer ribonucleic acid. Recognition of methionine by Escherichia coli methionyl-transfer ribonucleic acid synthetase.转移核糖核酸的氨酰化作用。大肠杆菌甲硫氨酰转移核糖核酸合成酶对甲硫氨酸的识别。

Biochem J. 1977 Aug 1;165(2):367-73. doi: 10.1042/bj1650367.

Interrelation between transfer RNA and amino-acid-activating sites of methionyl transfer RNA synthetase from Escherichia coli.大肠杆菌甲硫氨酰转运RNA合成酶的转运RNA与氨基酸激活位点之间的相互关系

Eur J Biochem. 1977 Oct 3;79(2):433-41. doi: 10.1111/j.1432-1033.1977.tb11825.x.

Neutron-scattering studies of the binding of initiator tRNAMet to escherichia coli trypsin modified methionyl-tRNA synthetase.起始tRNA甲硫氨酸与经大肠杆菌胰蛋白酶修饰的甲硫氨酰-tRNA合成酶结合的中子散射研究

J Mol Biol. 1982 Feb 5;154(4):603-13. doi: 10.1016/s0022-2836(82)80017-x.

Couplings between the sites for methionine and adenosine 5'-triphosphate in the amino acid activation reaction catalyzed by trypsin-modified methionyl-transfer RNA synthetase from Escherichia coli.来自大肠杆菌的经胰蛋白酶修饰的甲硫氨酰 - 转移RNA合成酶所催化的氨基酸活化反应中，甲硫氨酸位点与腺苷5'-三磷酸位点之间的偶联。

Biochemistry. 1977 May 31;16(11):2570-9. doi: 10.1021/bi00630a039.

Interaction between dimeric methionyl-tRNA synthetase and methionine accepting tRNAs from E. coli.-- Studies by partial ribonuclease digestion.二聚体甲硫氨酰 - tRNA合成酶与来自大肠杆菌的甲硫氨酸接纳tRNA之间的相互作用——部分核糖核酸酶消化研究

Biochimie. 1984 Sep-Oct;66(9-10):625-30. doi: 10.1016/0300-9084(84)90116-0.

31P NMR of the reversible methionine activation reaction catalyzed by methionyl-tRNA synthetase of Escherichia coli. Equilibrium, interconversion rates, and NMR parameters of the enzyme-bound species.大肠杆菌甲硫氨酰 - tRNA合成酶催化的可逆甲硫氨酸活化反应的31P核磁共振研究。酶结合物的平衡、相互转化率及核磁共振参数。

J Biol Chem. 1980 Sep 10;255(17):8164-9.

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Mol Gen Genet. 1982;186(2):263-8. doi: 10.1007/BF00331860.

The relA locus and the regulation of lysine biosynthesis in Escherichia coli.大肠杆菌中relA基因座与赖氨酸生物合成的调控

Mol Gen Genet. 1980;179(2):319-25. doi: 10.1007/BF00425459.

Mutations in the spoT gene of Salmonella typhimurium: effects on his operon expression.鼠伤寒沙门氏菌spoT基因的突变：对组氨酸操纵子表达的影响。

J Bacteriol. 1985 Aug;163(2):534-42. doi: 10.1128/jb.163.2.534-542.1985.

Growth inhibition as a consequence of antagonism between related amino acids: effect of valine in Escherichia coli K-12.相关氨基酸之间的拮抗作用导致的生长抑制：缬氨酸对大肠杆菌K-12的影响。

Microbiol Rev. 1979 Mar;43(1):42-58. doi: 10.1128/mr.43.1.42-58.1979.

The relA locus specifies a positive effector in branched-chain amino acid transport regulation.relA基因座在支链氨基酸转运调节中指定一种正效应物。

J Bacteriol. 1979 Feb;137(2):1059-62. doi: 10.1128/jb.137.2.1059-1062.1979.

Correlation between the serine sensitivity and the derepressibility of the ilv genes in Escherichia coli relA- mutants.大肠杆菌relA-突变体中丝氨酸敏感性与ilv基因去阻遏性之间的相关性。

Mol Gen Genet. 1978 Sep 20;165(1):21-30. doi: 10.1007/BF00270372.

In vitro synthesis of cystathionine gamma-synthetase in Escherichia coli K-12.大肠杆菌K-12中胱硫醚γ-合成酶的体外合成

J Bacteriol. 1978 Mar;133(3):1351-7. doi: 10.1128/jb.133.3.1351-1357.1978.

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