The Escherichia coli orthologue of the Salmonella ushB gene (ushBc) produces neither UDP-sugar hydrolase activity nor detectable protein, but has an identical sequence to that of Escherichia coli cdh

Schroder, Wayne A.

doi:10.1016/s0378-1097(01)00335-4

Cited by 1 publication

(1 citation statement)

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“…Another possible situation is represented by the ushB gene of Salmonella (encoding a UDP–sugar‐hydrolase), which has an orthologue, ushB ( c ) in E. coli , which does not produce this enzyme activity. In fact the ushB ( c ) gene shares 100% identity with the E. coli gene for CDP‐diglyceride hydrolase ( cdh ) but the ushB ( c ) gene does not produce any detectable protein in vivo despite being transcribed normally [110]. The possibility thus remains that the sequences found in obligate autotrophs and methanotrophs, seemingly encoding the E1 of α‐ketoglutarate dehydrogenase may in fact not even be capable of that function if expressed.…”

Section: Testing the α‐Ketoglutarate Hypothesismentioning

confidence: 99%

A challenge for 21st century molecular biology and biochemistry: what are the causes of obligate autotrophy and methanotrophy?

Wood¹,

Aurikko²,

Kelly³

2004

FEMS Microbiol Rev

163

113

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We assess the use to which bioinformatics in the form of bacterial genome sequences, functional gene probes and the protein sequence databases can be applied to hypotheses about obligate autotrophy in eubacteria. Obligate methanotrophy and obligate autotrophy among the chemo- and photo-lithotrophic bacteria lack satisfactory explanation a century or more after their discovery. Various causes of these phenomena have been suggested, which we review in the light of the information currently available. Among these suggestions is the absence in vivo of a functional alpha-ketoglutarate dehydrogenase. The advent of complete and partial genome sequences of diverse autotrophs, methylotrophs and methanotrophs makes it possible to probe the reasons for the absence of activity of this enzyme. We review the role and evolutionary origins of the Krebs cycle in relation to autotrophic metabolism and describe the use of in silico methods to probe the partial and complete genome sequences of a variety of obligate genera for genes encoding the subunits of the alpha-ketoglutarate dehydrogenase complex. Nitrosomonas europaea and Methylococcus capsulatus, which lack the functional enzyme, were found to contain the coding sequences for the E1 and E2 subunits of alpha-ketoglutarate dehydrogenase. Comparing the predicted physicochemical properties of the polypeptides coded by the genes confirmed the putative gene products were similar to the active alpha-ketoglutarate dehydrogenase subunits of heterotrophs. These obligate species are thus genomically competent with respect to this enzyme but are apparently incapable of producing a functional enzyme. Probing of the full and incomplete genomes of some cyanobacterial and methanogenic genera and Aquifex confirms or suggests the absence of the genes for at least one of the three components of the alpha-ketoglutarate dehydrogenase complex in these obligate organisms. It is recognized that absence of a single functional enzyme may not explain obligate autotrophy in all cases and may indeed be only be one of a number of controls that impose obligate metabolism. Availability of more genome sequences from obligate genera will enable assessment of whether obligate autotrophy is due to the absence of genes for a few or many steps in organic compound metabolism. This problem needs the technologies and mindsets of the present generation of molecular microbiologists to resolve it.

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Section: Testing the α‐Ketoglutarate Hypothesismentioning

confidence: 99%