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

Applied and environmental microbiology ·Vol. 57 ·No. 8 ·1991-08-00 ·Pages 2413-7

Kim SF, Baek SJ, Pack MY

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.

MeSH Terms

Amino Acid Sequence Base Sequence Cloning, Molecular DNA, Bacterial L-Lactate Dehydrogenase/genetics Lactobacillus casei/enzymology,genetics,growth & development Molecular Sequence Data

Chemicals

DNA, Bacterial L-Lactate Dehydrogenase

Authors & Affiliations

3 authors, click to expand affiliations / ORCID

Kim S F

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

Baek S J

Pack M Y

References (27)

27 references, click to expand

Transcription termination and the regulation of gene expression.
Annu Rev Biochem. 1986;55:339-72 PMID: 3527045
Cloning, expression and complete nucleotide sequence of the Bacillus stearothermophilus L-lactate dehydrogenase gene.
Gene. 1986;46(1):47-55 PMID: 3026926
Improved M13 phage cloning vectors and host strains: nucleotide sequences of the M13mp18 and pUC19 vectors.
Gene. 1985;33(1):103-19 PMID: 2985470
Sequence and characteristics of the Bifidobacterium longum gene encoding L-lactate dehydrogenase and the primary structure of the enzyme: a new feature of the allosteric site.
Gene. 1989 Dec 21;85(1):161-8 PMID: 2695396
From analysis to synthesis: new ligand binding sites on the lactate dehydrogenase framework. Part II.
Trends Biochem Sci. 1989 Apr;14(4):145-8 PMID: 2658222
From analysis to synthesis: new ligand binding sites on the lactate dehydrogenase framework. Part I.
Trends Biochem Sci. 1989 Mar;14(3):101-5 PMID: 2658216
A specific, highly active malate dehydrogenase by redesign of a lactate dehydrogenase framework.
Science. 1988 Dec 16;242(4885):1541-4 PMID: 3201242
Rational construction of a 2-hydroxyacid dehydrogenase with new substrate specificity.
Biochem Biophys Res Commun. 1987 Oct 14;148(1):15-23 PMID: 3314868
Oligonucleotide probes for the screening of recombinant DNA libraries.
Methods Enzymol. 1987;152:432-42 PMID: 3309569
Nucleotide sequence and characteristics of the gene for L-lactate dehydrogenase of Thermus caldophilus GK24 and the deduced amino-acid sequence of the enzyme.
Eur J Biochem. 1986 Oct 15;160(2):433-40 PMID: 3533539
The initiation of translation in E. coli: apparent base pairing between the 16srRNA and downstream sequences of the mRNA.
Nucleic Acids Res. 1990 Apr 11;18(7):1719-23 PMID: 2186363
The anti-Shine-Dalgarno region in Escherichia coli 16S ribosomal RNA is not essential for the correct selection of translational starts.
Biochemistry. 1990 Apr 3;29(13):3402-7 PMID: 2185838
Nucleotide sequence and characteristics of the gene for L-lactate dehydrogenase of Thermus aquaticus YT-1 and the deduced amino acid sequence of the enzyme.
J Biochem. 1990 Jan;107(1):21-6 PMID: 2185236
The pUC plasmids, an M13mp7-derived system for insertion mutagenesis and sequencing with synthetic universal primers.
Gene. 1982 Oct;19(3):259-68 PMID: 6295879
Compilation and analysis of Escherichia coli promoter DNA sequences.
Nucleic Acids Res. 1983 Apr 25;11(8):2237-55 PMID: 6344016
Nucleotide sequences that signal the initiation of transcription and translation in Bacillus subtilis.
Mol Gen Genet. 1982;186(3):339-46 PMID: 6181373
Structure-function relationship in the allosteric L-lactate dehydrogenases from Lactobacillus casei and Lactobacillus curvatus.
Eur J Biochem. 1982 Sep 1;126(3):549-58 PMID: 6814908
Affinity labelling of the allosteric site of the L-lactate dehydrogenase of Lactobacillus casei.
Eur J Biochem. 1983 Sep 15;135(2):359-65 PMID: 6411472
The complete primary structure of the allosteric L-lactate dehydrogenase from Lactobacillus casei.
Eur J Biochem. 1983 Aug 15;134(3):503-11 PMID: 6411465
Galactose fermentation by Streptococcus lactis and Streptococcus cremoris: pathways, products, and regulation.
J Bacteriol. 1980 Nov;144(2):672-82 PMID: 6776093
Effect of environmental pH on fermentation balance of Lactobacillus bulgaricus.
J Bacteriol. 1980 Oct;144(1):217-21 PMID: 7419489
Structural adaptations of lactate dehydrogenase isozymes.
Proc Natl Acad Sci U S A. 1977 Jul;74(7):2677-81 PMID: 197516
Change from homo- to heterolactic fermentation by Streptococcus lactis resulting from glucose limitation in anaerobic chemostat cultures.
J Bacteriol. 1979 Apr;138(1):109-17 PMID: 108249
Comparative studies of lactic acid dehydrogenases in lactic acid bacteria. I. Purification and kinetics of the allosteric L-lactic acid dehydrogenase from Lactobacillus casei ssp. casei and Lactobacillus curvatus.
Arch Microbiol. 1977 Feb 4;112(1):81-93 PMID: 14601
DNA sequencing with chain-terminating inhibitors.
Proc Natl Acad Sci U S A. 1977 Dec;74(12):5463-7 PMID: 271968
The 3'-terminal sequence of Escherichia coli 16S ribosomal RNA: complementarity to nonsense triplets and ribosome binding sites.
Proc Natl Acad Sci U S A. 1974 Apr;71(4):1342-6 PMID: 4598299
Evidence for extrachromosomal elements in Lactobacillus.
J Bacteriol. 1976 Sep;127(3):1576-8 PMID: 821936

Article Info

Journal

Applied and environmental microbiology

Abbr.

Appl Environ Microbiol

ISSN

0099-2240

DOI

10.1128/aem.57.8.2413-2417.1991

Published

1991-08-00

Pages

2413-7

Language

English

Region

United States

NLM ID

7605801

PMCID

PMC183587

Subset

Databases

GENBANK

M63813, M63814, M64340, M76708, S77578, X53167, X53168, X53169, X53170, X53171

External Links

PubMed source DOI: 10.1128/aem.57.8.2413-2417.1991 PMC Full Text View journal details

Analysis Services

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

Contact

WeChat Official Account