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铜绿假单胞菌中精氨酸生物合成的基因组织。

The genetic organization of arginine biosynthesis in Pseudomonas aeruginosa.

作者信息

Haas D, Holloway B W, Schamböck A, Leisinger T

出版信息

Mol Gen Genet. 1977 Jul 7;154(1):7-22. doi: 10.1007/BF00265571.

Abstract

Six loci coding for arginine biosynthetic enzymes in Pseudomonas aeruginosa strain PAO were identified by enzyme assay: argA (N-acetylglutamate synthase), argB (N-acetylglutamate 5-phosphotransferase), argC (N-acetylglutamate 5-semialdehyde dehydrogenase), argF (anabolic ornithine carbamoyl-transferase), argG (argininosuccinate synthetase), and argH (argininosuccinase). One-step mutants which had a requirement for arginine and uracil were defective in carbamoylphosphate synthase, specified by a locus designated car. To map these mutations we used the sex factor FP2 in an improved interrupted mating technique as well as the generalized transducing phages F116L and G101. We confirmed earlier studies, and found no clustering of arg and car loci. However, argA, argH, and argB were mapped on a short chromosome segment (approx. 3 min long), and argF and argG were cotransducible, but not contiguous. N-Acetylglutamate synthase, the enzyme which replenishes the cycle of acetylated intermediates in ornithine synthesis of Pseudomonas, appears to be essential for arginine synthesis since argA mutants showed no growth on unsupplemented minimal medium.

摘要

通过酶活性测定,在铜绿假单胞菌PAO菌株中鉴定出六个编码精氨酸生物合成酶的基因座:argA(N-乙酰谷氨酸合酶)、argB(N-乙酰谷氨酸5-磷酸转移酶)、argC(N-乙酰谷氨酸5-半醛脱氢酶)、argF(合成鸟氨酸氨甲酰转移酶)、argG(精氨琥珀酸合成酶)和argH(精氨琥珀酸酶)。对精氨酸和尿嘧啶有需求的一步突变体在氨甲酰磷酸合酶方面存在缺陷,该酶由一个名为car的基因座所指定。为了定位这些突变,我们在一种改进的中断杂交技术中使用了性因子FP2以及广义转导噬菌体F116L和G101。我们证实了早期的研究结果,并且发现arg和car基因座没有聚集现象。然而,argA、argH和argB被定位在一个短的染色体片段上(大约3分钟长),并且argF和argG是共转导的,但并不相邻。N-乙酰谷氨酸合酶是在假单胞菌鸟氨酸合成中补充乙酰化中间体循环的酶,由于argA突变体在未补充的基本培养基上无法生长,所以它似乎对精氨酸合成至关重要。

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