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干酪乳杆菌乳酸脱氢酶基因的克隆与核苷酸序列分析

Cloning and nucleotide sequence of the Lactobacillus casei lactate dehydrogenase gene.

作者信息

Kim S F, Baek S J, Pack M Y

机构信息

Department of Biological Science and Engineering, Korea Advanced Institute of Science and Technology, Seoul.

出版信息

Appl Environ Microbiol. 1991 Aug;57(8):2413-7. doi: 10.1128/aem.57.8.2413-2417.1991.

DOI:10.1128/aem.57.8.2413-2417.1991
PMID:1768113
原文链接:https://pmc.ncbi.nlm.nih.gov/articles/PMC183587/
Abstract

An allosteric L-(+)-lactate dehydrogenase gene of Lactobacillus casei ATCC 393 was cloned in Escherichia coli, and the nucleotide sequence of the gene was determined. The gene was composed of an open reading frame of 981 bp, starting with a GTG codon and ending with a TAA codon. The sequences for the promoter and ribosome binding site were identified, and a sequence for a structure resembling a rho-independent transcription terminator was also found.

摘要

干酪乳杆菌ATCC 393的一种变构L-(+)-乳酸脱氢酶基因在大肠杆菌中被克隆，并测定了该基因的核苷酸序列。该基因由一个981 bp的开放阅读框组成，起始密码子为GTG，终止密码子为TAA。确定了启动子和核糖体结合位点的序列，还发现了一个类似于不依赖ρ因子的转录终止子结构的序列。

https://cdn.ncbi.nlm.nih.gov/pmc/blobs/909f/183587/0040809bee0a/aem00061-0315-a.jpg
https://cdn.ncbi.nlm.nih.gov/pmc/blobs/909f/183587/0040809bee0a/aem00061-0315-a.jpg
https://cdn.ncbi.nlm.nih.gov/pmc/blobs/909f/183587/0040809bee0a/aem00061-0315-a.jpg

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