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Identification and molecular modeling of a novel lipase from an Antarctic soil metagenomic library

100%

Cieslinski H., Bialkowska A., Tkaczuk K., Dlugolecka A., Kur J., Turkiewicz M.

Polish Journal of Microbiology

2009

tom 58

nr 3

199-204

In this work, we present the construction of a metagenomic library in Escherichia coli using pUC19 vector and environmental DNA directly isolated from Antarctic topsoil and screened for lipolytic enzymes. Screening on agar supplemented with olive oil and rhodamine B revealed one clone with lipolytic activity (Lip 1) out of 11000 E. coli clones. This clone harbored a plasmid, pLip 1, which has an insert of 4722 bp that was completely sequenced from both directions. Further analysis of the insert showed three open reading frames (ORFs). ORF2 encoded a protein (Lip 1) of 469 amino acids with 93% identity to the uncultured Pseudomonas sp. lipase LipJ03. Amino acid sequence comparison and phylogenetic analysis indicated that Lip 1 lipase was closely related to family I subfamily 3. Furthermore, we present a three-dimensional model of lipase Lip 1 which was generated based on the two known structures of mesophilic lipases from Pseudomonas sp. MIS 38 (PML lipase, PDB; 2Z8X) and Seiratia marcescens (SML lipase, PDB: 2QUB). Finally, we report the results of comparisons between lipase Lip 1 and mesophilic lipases and point out similarities and differences in the catalytic site and in other parts of the analyzed structures.

Identification of the csp gene and molecular modelling of the CspA-like protein from Antarctic soil-dwelling psychrotrophic bacterium Psychrobacter sp. B6

88%

Kaufman-Szymczyk A., Wojtasik A., Parniewski P., Bialkowska A., Tkaczuk K., Turkiewicz M.

Acta Biochimica Polonica

2009

tom 56

nr 1

63-69

We cloned and sequenced the cspA-like gene from a psychrotrophic Antarctic soil-dwelling bacterial strain Psychrobacter sp. B6. The gene is 213 bp long and shows 99% and 98% sequence identity with the Psychrobacter cryohalolentis K5 gene encoding a cold-shock DNA-binding domain protein and the Psychrobacter arcticus transcriptional regulator-CspA gene, respectively. The protein encoded by the Psychrobacter sp. B6 cspA-like gene shows 100% identity with the two proteins mentioned above, and also 61% sequence identity with CspB from Bacillus subtilis and Csp from Bacillus caldolyticus, and 56% — with Escherichia coli CspA protein. A three-dimensional model of the CspA-like protein from Psychrobacter sp. B6 was generated based on three known structures of cold shock proteins: the crystal structure of the major cold shock protein from Escherichia coli (CspA), the NMR structure of the latter protein, and the NMR structure of Csp from Thermotoga maritima. The deduced structure of the CspA-like protein from Psychrobacter sp. B6 was found to be very similar to these known structures of Csp-like proteins.

Ograniczanie wyników

1 Acta Biochimica Polonica

1 Polish Journal of Microbiology

2 Bialkowska A.

2 Tkaczuk K.

2 Turkiewicz M.

1 Cieslinski H.

1 Dlugolecka A.

1 Kaufman-Szymczyk A.

1 Kur J.

1 Parniewski P.

1 Wojtasik A.

2 2009

Wyniki wyszukiwania

Identification and molecular modeling of a novel lipase from an Antarctic soil metagenomic library

Identification of the csp gene and molecular modelling of the CspA-like protein from Antarctic soil-dwelling psychrotrophic bacterium Psychrobacter sp. B6