Genetic organization of the mle locus and identification of a mleR-like gene from Leuconostoc oenos

Article Abstract:

The characterization of the mle locus from Leuconostoc oenos shows a 2.6-kb transcript, indicating that it may have an operon structure containing the malolactic enzyme gene mleA and malate permease gene mleP. The mle operon has one transcription start site situated 17 nucleotides upstream of the ATG translation start site for the mleA gene. An 894-bp open reading frame (RF), that transcribes divergently from the mle operon, is located upstream of the mleA gene. This ORF encodes a polypeptide belonging to the LysR-type regulatory protein family, and has a molecular mass of 34 kDa.

author: Divies, Charles, Guzzo, Jean, Labarre, Cecile
Observations, Microbial enzymes, Genetic transcription, Operons, Transcription (Genetics)

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Molecular characterization of the gene encoding an 18-kilodalton small heat shock protein associated with the membrane of Leuconostoc oenos

Article Abstract:

The hsp18 gene encodes a small heat shock 18-kilodalton polypeptide Lo18, that is peripherally associated with the membrane of Leuconostoc oenos. The transcription of this heat shock gene increases with an increase in temperature. The gene forms a unique transcription unit in L. oenos that is similar to the unit in Clostridium acetobutylicum and Streptomyces albus. The gene has a putative promoter whose structure is similar to the consensus promoter sequence of vegetative genes of both gram-negative and gram-positive bacteria.

author: Divies, Charles, Guzzo, Jean, Garmyn, Dominique, Jobin, Michel-Philippe, Delmas, Francoise
Analysis, Amino acid sequence, Amino acid sequencing

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Expression of the Oenococcus oeni trxA gene is induced by hydrogen peroxide and heat shock

Article Abstract:

A study was conducted to analyze the nucleotide sequence of a chromosomal DNA fragment encoding the thioredoxin of Oenococcus oeni. The size of the transcript and the transcriptional start site were determined. The expression of the gene in response to oxidative and heat stresses were then analyzed. Experimental results indicated that the trxA gene encodes a functional thioredoxin.

author: Divies, Charles, Guzzo, Jean, Garmyn, Dominique, Jobin, Michel-Philippe
Physiological aspects, DNA, Bacteria, Lactic acid, Proteins, Hydrogen peroxide

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subjects list: Research, Heat shock proteins
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