Evidence map›Paper›PMID 16391068›Full record

ArticleApplied and environmental microbiology2006

Isolation of poly-3-hydroxybutyrate metabolism genes from complex microbial communities by phenotypic complementation of bacterial mutants.

Chunxia Wang, David J Meek, Priya Panchal, Natalie Boruvka, Frederick S Archibald, Brian T Driscoll, Trevor C Charles

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Article in Applied and environmental microbiology, 2006. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 17 papers.

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17citing papers in PubMed
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1 · What the graph read from it

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2 · The registry

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3 · Its place in the literature

Who cites it

17 citing papers in PubMed.

  1. Article
  2. The transport of mannitol inMicrobiology (Reading, England) · 2023
    Article
  3. Article
  4. Article
  5. Review
  6. Article
  7. Article
  8. Review
  9. Article
  10. Article
  11. Metagenomic analyses: past and future trends.Applied and environmental microbiology · 2011
    Review
  12. Article
  13. Article
  14. Article
  15. Achievements and new knowledge unraveled by metagenomic approaches.Applied microbiology and biotechnology · 2009
    Review
  16. Article
  17. Article
4 · The record

Corrections and comments

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5 · Who and what money

Authors and funding

7 authors.

Chunxia WangDepartment of Biology, University of Waterloo, 200 University Ave. West, Waterloo, ON N2L 3G1, Canada.
David J Meek
Priya Panchal
Natalie Boruvka
Frederick S Archibald
Brian T Driscoll
Trevor C Charles

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

The goal of this study was to initiate investigation of the genetics of bacterial poly-3-hydroxybutyrate (PHB) metabolism at the community level. We constructed metagenome libraries from activated sludge and soil microbial communities in the broad-host-range IncP cosmid pRK7813. Several unique clones were isolated from these libraries by functional heterologous complementation of a Sinorhizobium meliloti bdhA mutant, which is unable to grow on the PHB cycle intermediate D-3-hydroxybutyrate due to absence of the enzyme D-3-hydroxybutyrate dehydrogenase activity. Clones that conferred D-3-hydroxybutyrate utilization on Escherichia coli were also isolated. Although many of the S. meliloti bdhA mutant complementing clones restored D-3-hydroxybutyrate dehydrogenase activity to the mutant host, for some of the clones this activity was not detectable. This was also the case for almost all of the clones isolated in the E. coli selection. Further analysis was carried out on clones isolated in the S. meliloti complementation. Transposon mutagenesis to locate the complementing genes, followed by DNA sequence analysis of three of the genes, revealed coding sequences that were broadly divergent but lay within the diversity of known short-chain dehydrogenase/reductase encoding genes. In some cases, the amino acid sequence identity between pairs of deduced BdhA proteins was <35%, a level at which detection by nucleic acid hybridization based methods would probably not be successful.

Indexed as

Genetic Complementation TestMutationSoil MicrobiologyCloning, MolecularCytophagaGene LibraryGram-Negative BacteriaHydroxybutyrate DehydrogenaseHydroxybutyratesMolecular Sequence DataPhenotypePlasmidsPolyestersPolyhydroxybutyratesProteobacteriaRNA, Ribosomal, 16SHydroxybutyrate DehydrogenaseHydroxybutyratespoly-beta-hydroxybutyratePolyestersPolyhydroxybutyratesRNA, Ribosomal, 16SSewage

Identifiers

PMID16391068
PMCPMC1352230

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Read under generation 80e0d062 · epoch 390. Bibliography from PubMed, PubMed Central and OpenAlex; grants from NIH RePORTER; trial links from ClinicalTrials.gov; estimates, votes and beliefs from the OpenQuestion graph.