Document Detail


The complete genome of Rhodococcus sp. RHA1 provides insights into a catabolic powerhouse.
MedLine Citation:
PMID:  17030794     Owner:  NLM     Status:  MEDLINE    
Abstract/OtherAbstract:
Rhodococcus sp. RHA1 (RHA1) is a potent polychlorinated biphenyl-degrading soil actinomycete that catabolizes a wide range of compounds and represents a genus of considerable industrial interest. RHA1 has one of the largest bacterial genomes sequenced to date, comprising 9,702,737 bp (67% G+C) arranged in a linear chromosome and three linear plasmids. A targeted insertion methodology was developed to determine the telomeric sequences. RHA1's 9,145 predicted protein-encoding genes are exceptionally rich in oxygenases (203) and ligases (192). Many of the oxygenases occur in the numerous pathways predicted to degrade aromatic compounds (30) or steroids (4). RHA1 also contains 24 nonribosomal peptide synthase genes, six of which exceed 25 kbp, and seven polyketide synthase genes, providing evidence that rhodococci harbor an extensive secondary metabolism. Among sequenced genomes, RHA1 is most similar to those of nocardial and mycobacterial strains. The genome contains few recent gene duplications. Moreover, three different analyses indicate that RHA1 has acquired fewer genes by recent horizontal transfer than most bacteria characterized to date and far fewer than Burkholderia xenovorans LB400, whose genome size and catabolic versatility rival those of RHA1. RHA1 and LB400 thus appear to demonstrate that ecologically similar bacteria can evolve large genomes by different means. Overall, RHA1 appears to have evolved to simultaneously catabolize a diverse range of plant-derived compounds in an O(2)-rich environment. In addition to establishing RHA1 as an important model for studying actinomycete physiology, this study provides critical insights that facilitate the exploitation of these industrially important microorganisms.
Authors:
Michael P McLeod; René L Warren; William W L Hsiao; Naoto Araki; Matthew Myhre; Clinton Fernandes; Daisuke Miyazawa; Wendy Wong; Anita L Lillquist; Dennis Wang; Manisha Dosanjh; Hirofumi Hara; Anca Petrescu; Ryan D Morin; George Yang; Jeff M Stott; Jacqueline E Schein; Heesun Shin; Duane Smailus; Asim S Siddiqui; Marco A Marra; Steven J M Jones; Robert Holt; Fiona S L Brinkman; Keisuke Miyauchi; Masao Fukuda; Julian E Davies; William W Mohn; Lindsay D Eltis
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Publication Detail:
Type:  Journal Article; Research Support, Non-U.S. Gov't     Date:  2006-10-09
Journal Detail:
Title:  Proceedings of the National Academy of Sciences of the United States of America     Volume:  103     ISSN:  0027-8424     ISO Abbreviation:  Proc. Natl. Acad. Sci. U.S.A.     Publication Date:  2006 Oct 
Date Detail:
Created Date:  2006-10-18     Completed Date:  2007-01-26     Revised Date:  2010-09-15    
Medline Journal Info:
Nlm Unique ID:  7505876     Medline TA:  Proc Natl Acad Sci U S A     Country:  United States    
Other Details:
Languages:  eng     Pagination:  15582-7     Citation Subset:  IM    
Affiliation:
Department of Microbiology and Immunology, Life Sciences Institute, University of British Columbia, Vancouver, BC, Canada V6T 1Z3.
Data Bank Information
Bank Name/Acc. No.:
RefSeq/NC_008268;  NC_008269;  NC_008270;  NC_008271
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MeSH Terms
Descriptor/Qualifier:
Bacterial Proteins* / classification,  genetics
Chromosome Mapping
Evolution
Genome, Bacterial*
Metabolism*
Molecular Sequence Data
Phylogeny
Rhodococcus* / genetics,  metabolism
Chemical
Reg. No./Substance:
0/Bacterial Proteins
Comments/Corrections

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