Article Abstract:
The lipase encoding gene (lipA) was isolated from a genomic library of a psychrotrophic lipolytic Pseudomonas strain LS107d2. The nucleotide sequence of the gene showed an open reading frame of 1,412 bp, encoding a peptide with an estimated mass of 49,905. The expressed lipase had a molecular mass of 50,000. Amino acid sequence deduced from the nucleotide sequence showed no extensive similarity to lipases from P. cepacia and P. fragi. Escherichia coli transformed for this gene expressed the polypeptide in the cytoplasm, although this intracytoplasmic lipase is probably inactive.
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Article Abstract:
Experiments were conducted to clone the ligZ gene encoding a ring cleavage enzyme for 2,2',3-trihydroxy-3'-methoxy-5,5'-dicarboxybiphenyl (OH-DDVA) oxygenase gene of Sphingomonas paucimobilis. An OH-DDVA and DDVA growth-deficient mutant was created by mutagenesis to identify the gene responsible for the ring cleavage. Deletions in the gene fragment were constructed and their oxygen consumption activity was studied. The fragments exhibited two open reading frames with overlapping and opposing transcriptional directions.
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Article Abstract:
A transposon-induced NaCl-sensitive mutant of the highly halotolerant, nonhalophilic bacteria Staphylococcus aureus was characterized by cloning, sequencing and analyzing the mutated gene brnQ with the flanking sequences of the transposon at the mutant's insertion site. The mutation of the gene, which encodes a branched-chain-amino-acid transport protein of S. aureus, is the cause of the bacteria's NaCl-sensitive phenotype.
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