Cloning and sequencing of the Sphingomonas (Pseudomonas) paucimobilis gene essential for the O demethylation of vanillate and syringate

Sphingomonas (Pseudomonas) paucimobilis SYK-6 is able to grow on 5,5'-dehydrodivanillic acid (DDVA), syringate, vanillate, and other dimeric model compounds of lignin as a sole carbon source. Nitrosoguanidine mutagenesis of S. paucimobilis SYK-6 was performed, and two mutants with altered DDVA...

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Bibliographic Details
Published in:Applied and environmental microbiology 1998-03, Vol.64 (3), p.836-842
Main Authors: NISHIKAWA, S, SONOKI, T, KASAHARA, T, OBI, T, KUBOTA, S, KAWAI, S, MOROHOSHI, N, KATAYAMA, Y
Format: Article
Language:English
Subjects:
Amino Acid Sequence
Biological and medical sciences
Biology
Biology of microorganisms of confirmed or potential industrial interest
Biotechnology
Cloning
Cloning, Molecular
Dealkylation
DNA, Bacterial - chemistry
Fundamental and applied biological sciences. Psychology
Gallic Acid - analogs & derivatives
Gallic Acid - metabolism
Genes, Bacterial
Genetics
Genetics and Molecular Biology
Lignin - metabolism
Mission oriented research
Molecular Sequence Data
Mutation
Pseudomonas - genetics
Vanillic Acid - metabolism
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Summary:Sphingomonas (Pseudomonas) paucimobilis SYK-6 is able to grow on 5,5'-dehydrodivanillic acid (DDVA), syringate, vanillate, and other dimeric model compounds of lignin as a sole carbon source. Nitrosoguanidine mutagenesis of S. paucimobilis SYK-6 was performed, and two mutants with altered DDVA degradation pathways were isolated. The mutant strain NT-1 could not degrade DDVA, but could degrade syringate, vanillate, and 2,2',3'-trihydroxy-3-methoxy-5,5'-dicarboxybiphenyl (OH-DDVA). Strain DC-49 could slowly assimilate DDVA, but could degrade neither vanillate nor syringate, although it could degrade protocatechuate and 3-O-methylgallate. A complementing DNA fragment of strain DC-49 was isolated from the cosmid library of strain SYK-6. The minimum DNA fragment complementing DC-49 was determined to be the 1.8-kbp insert of pKEX2.0. Sequencing analysis showed an open reading frame of 1,671 bp in this fragment, and a similarity search indicated that the deduced amino acid sequence of this open reading frame had significant similarity (60%) to the formyltetrahydrofolate synthetase of Clostridium thermoaceticum.
ISSN:0099-2240
1098-5336
DOI:10.1128/aem.64.3.836-842.1998