Genomic analysis of carbon source metabolism of Shewanella oneidensis MR-1:: Predictions versus experiments

被引:82
作者
Serres, Margrethe H. [1 ]
Riley, Monica [1 ]
机构
[1] Marine Biol Lab, Josephine Bay Paul Ctr Comparat Mol Biol & Evolut, Woods Hole, MA 02543 USA
关键词
D O I
10.1128/JB.01787-05
中图分类号
Q93 [微生物学];
学科分类号
071005 ; 100705 ;
摘要
Genomic sequences have been used to find the genetic foundation for carbon source metabolism in Shewanella oneidensis MR-1. Annotated S. oneidensis MR-1 gene products were examined for their sequence similarity to enzymes participating in pathways for utilization of carbon and energy as described in the BioCyc database (http://www.biocyc.org/) or in the primary literature. A picture emerges that relegates five- and six-carbon sugars to minor roles as carbon sources, whereas multiple pathways for utilization of up to three-carbon carbohydrates seem to be present. Capacity to utilize amino acids for carbon and energy is also present. A few contradictions emerged in which enzymes appear to be present by annotations but are not active in the cell according to physiological experiments. Annotations are based on close sequence similarity and will not reveal inactivity due to deleterious mutations or due to lack of coordination of regulation and transport. Genes for a few enzymes known by experiment to be active are not found in the genome. This may be due to extensive divergence after duplication or convergence of function in separate lines in evolution rendering activities undetectable by sequence similarity. To minimize false predictions from protein sequences, we have been conservative in predicting pathways. We did not predict any pathway when, although a partial pathway was seen it was composed largely of enzymes already accounted for in any other complete pathway. This is an example of how a biochemically oriented sequence analysis can generate questions and direct further experimental investigation.
引用
收藏
页码:4601 / 4609
页数:9
相关论文
共 25 条
[1]   AMINO-ACID SUBSTITUTION MATRICES FROM AN INFORMATION THEORETIC PERSPECTIVE [J].
ALTSCHUL, SF .
JOURNAL OF MOLECULAR BIOLOGY, 1991, 219 (03) :555-565
[2]   Metal oxide surfaces and their interactions with aqueous solutions and microbial organisms [J].
Brown, GE ;
Henrich, VE ;
Casey, WH ;
Clark, DL ;
Eggleston, C ;
Felmy, A ;
Goodman, DW ;
Grätzel, M ;
Maciel, G ;
McCarthy, MI ;
Nealson, KH ;
Sverjensky, DA ;
Toney, MF ;
Zachara, JM .
CHEMICAL REVIEWS, 1999, 99 (01) :77-174
[3]   A rare cause of wound infection:: Shewanella putrefaciens [J].
Bulut, C ;
Ertem, GT ;
Gökcek, C ;
Tulek, N ;
Bayar, MA ;
Karakoc, E .
SCANDINAVIAN JOURNAL OF INFECTIOUS DISEASES, 2004, 36 (09) :692-694
[4]   Multiple formate dehydrogenase enzymes in the facultative methylotroph Methylobacterium extorquens AM1 are dispensable for growth on methanol [J].
Chistoserdova, L ;
Laukel, M ;
Portais, JC ;
Vorholt, JA ;
Lidstrom, ME .
JOURNAL OF BACTERIOLOGY, 2004, 186 (01) :22-28
[5]   Methylotrophy in Methylobacterium extorquens AM1 from a genomic point of view [J].
Chistoserdova, L ;
Chen, SW ;
Lapidus, A ;
Lidstrom, ME .
JOURNAL OF BACTERIOLOGY, 2003, 185 (10) :2980-2987
[6]  
Daraselia N., 2003, OMICS A Journal of Integrative Biology, V7, P171, DOI 10.1089/153623103322246566
[7]   Darwin v. 2.0: an interpreted computer language for the biosciences [J].
Gonnet, GH ;
Hallett, MT ;
Korostensky, C ;
Bernardin, L .
BIOINFORMATICS, 2000, 16 (02) :101-103
[8]   The acnD genes of Shewenella oneidensis and Vibrio cholerae encode a new Fe/S-dependent 2-methylcitrate dehydratase enzyme that requires prpF function in vivo [J].
Grimek, TL ;
Escalante-Semerena, JC .
JOURNAL OF BACTERIOLOGY, 2004, 186 (02) :454-462
[9]   Genome sequence of the dissimilatory metal ion-reducing bacterium Shewanella oneidensis [J].
Heidelberg, JF ;
Paulsen, IT ;
Nelson, KE ;
Gaidos, EJ ;
Nelson, WC ;
Read, TD ;
Eisen, JA ;
Seshadri, R ;
Ward, N ;
Methe, B ;
Clayton, RA ;
Meyer, T ;
Tsapin, A ;
Scott, J ;
Beanan, M ;
Brinkac, L ;
Daugherty, S ;
DeBoy, RT ;
Dodson, RJ ;
Durkin, AS ;
Haft, DH ;
Kolonay, JF ;
Madupu, R ;
Peterson, JD ;
Umayam, LA ;
White, O ;
Wolf, AM ;
Vamathevan, J ;
Weidman, J ;
Impraim, M ;
Lee, K ;
Berry, K ;
Lee, C ;
Mueller, J ;
Khouri, H ;
Gill, J ;
Utterback, TR ;
McDonald, LA ;
Feldblyum, TV ;
Smith, HO ;
Venter, JC ;
Nealson, KH ;
Fraser, CM .
NATURE BIOTECHNOLOGY, 2002, 20 (11) :1118-1123
[10]   Phylogenetic relationships among marine Alteromonas-like proteobacteria:: emended description of the family Alteromonadaceae and proposal of Pseudoalteromonadaceae fam. nov., Colwelliaceae fam. nov., Shewanellaceae fam. nov., Montellaceae fam. nov., Ferrimonadaceae fam. nov., Idiomarinaceae fam. nov and Psychromonadaceae fam. nov. [J].
Ivanova, EP ;
Flavier, S ;
Christen, R .
INTERNATIONAL JOURNAL OF SYSTEMATIC AND EVOLUTIONARY MICROBIOLOGY, 2004, 54 :1773-1788