Gene duplication in experimental enzyme evolution

Rigby, Peter; Burleigh, Bruce D.; Hartley, Brian

doi:10.1038/251200a0

Cited by 152 publications

(87 citation statements)

References 14 publications

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“…An example of increased activity of a catabolic enzyme leading to faster growth at low substrate concentrations is provided by the 'hyper ' mutants of Escherichia coli, which outgrew the wild type at low lactose concentrations, evidently because they synthesized increased levels of /3-galactosidase (Horiuchi, Tomizawa & Novick, 1962;Smith & Dean, 1972). The work of Rigby, Burleigh & Hartley (1974) illustrates the role of the affinity of a catabolic enzyme in the outcome of competition: a mutant of Klebsiella aerogenes possessing a lower K, for the first enzyme in xylitol metabolism (ribitol dehydrogenase) outcompeted the wild-type during xylitol-limited growth in a chemostat.…”

Section: Discussionmentioning

confidence: 99%

Physiological Basis of the Selective Advantage of a Spirillum sp. in a Carbon-limited Environment

Matin

Veldkamp

1978

Journal of General Microbiology

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Section: Discussionmentioning

confidence: 99%

Physiological Basis of the Selective Advantage of a Spirillum sp. in a Carbon-limited Environment

Matin

Veldkamp

1978

Journal of General Microbiology

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“…Further evolution of this ' silent gene ', initially silenced by a mutation causing reduced transcription or a reduced level of functional product, which is maintained in the population for a finite period of time, then ensues via accumulation of a variety of additional mutations. Eventually such a gene may be lost by deletion but, before this occurs, it may instead acquire a functional, albeit modified, enzymic form that will persist if of selective value to the cell (Koch, 1972 ;Hartley, 1974Hartley, , 1979Hartley, , 1980Hartley, , 1984Rigby et al, 1974 ;Beacham, 1987). The term ' silent gene ' has been previously used to include the possibility that, in one allele of the duplicates, lack of a functional gene product may also result from a missense mutation(s) causing, for example, aberrant folding of the encoded protein (Hartley, 1974 ;Rigby et al, 1974).…”

Section: Abbreviation : Et Electrophoretic Typementioning

confidence: 99%

“…Eventually such a gene may be lost by deletion but, before this occurs, it may instead acquire a functional, albeit modified, enzymic form that will persist if of selective value to the cell (Koch, 1972 ;Hartley, 1974Hartley, , 1979Hartley, , 1980Hartley, , 1984Rigby et al, 1974 ;Beacham, 1987). The term ' silent gene ' has been previously used to include the possibility that, in one allele of the duplicates, lack of a functional gene product may also result from a missense mutation(s) causing, for example, aberrant folding of the encoded protein (Hartley, 1974 ;Rigby et al, 1974). The high level of gene paralogy in prokaryotic genomes indicates that gene duplication is a major mechanism for generating biochemical diversity (Labedan & Riley, 1995 ;Riley & Labedan, 1997).…”

Section: Abbreviation : Et Electrophoretic Typementioning

confidence: 99%

The cryptic ushA gene (ushA c) in natural isolates of Salmonella enterica (serotype Typhimurium) has been inactivated by a single missense mutation The GenBank accession numbers for the sequences determined in this work are AF188721–AF188732.

et al. 2001

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Two mutational mechanisms, both supported by experimental studies, have been proposed for the evolution of new or improved enzyme specificities in bacteria. One mechanism involves point mutation(s) in a gene conferring novel substrate specificity with partial or complete loss of the original (wild-type) activity of the encoded product. The second mechanism involves gene duplication followed by silencing (inactivation) of one of these duplicates. Some of these ' silent genes ' may still be transcribed and translated but produce greatly reduced levels of functional protein ; gene silencing, in this context, is distinct from the more common associations with bacterial partitioning sequences, and with genes which are no longer transcribed or translated. Whereas most Salmonella enterica strains are ushA M , encoding an active 5'-nucleotidase (UDP-sugar hydrolase), some natural isolates, including most genetically related strains of serotype Typhimurium, have an ushA allele (designated ushA c ) which produces a protein with, comparatively, very low 5'-nucleotidase activity. Previous sequence analysis of cloned ushA c and ushA M genes from serotype Typhimurium strain LT2 and Escherichia coli, respectively, did not reveal any changes which might account for the significantly different 5'-nucleotidase activities. The mechanism responsible for this reduced activity of UshA c has hitherto not been known. Sequence analysis of Salmonella ushA M and ushA c alleles indicated that the relative inactivity of UshA c may be due to one, or more, of four amino acid substitutions. One of these changes (S139Y) is in a sequence motif that is conserved in 5'-nucleotidases across a range of diverse prokaryotic and eukaryotic species. Site-directed mutagenesis confirmed that a Tyr substitution of Ser-139 in Salmonella UshA M was solely responsible for loss of 5'-nucleotidase activity. It is concluded that the corresponding single missense mutation is the cause of the UshA c phenotype. This is the first reported instance of gene inactivation in natural isolates of bacteria via a missense mutation. These results support a model of evolution of new enzymes involving a ' silent gene ' which produces an inactive, or relatively inactive, product, and are also consistent with the evolution of a novel, but unknown, enzyme specificity by a single amino acid change.

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“…Indeed, it can be argued that the tolerance of variation in protein structure is what allows the process of random mutation and natural selection to proceed 3. Nonetheless, there are some proteins in which a small conformational change, such as the cis / trans isomerisation of a proline residue, is sufficient to modulate function 4, 5…”

mentioning

confidence: 99%

Refoldable Foldamers: Global Conformational Switching by Deletion or Insertion of a Single Hydrogen Bond

2016

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Small changes in the structure of a foldamer may lead to gross changes in conformational preference. We show that the simple insertion or deletion of a single hydrogen bond by changes in pH or by photochemical deprotection is sufficient to refold a helical oligomer, interconverting M and P screw‐sense preference. As a consequence of the switch, information may be transmitted to a remote catalytic site, selectively directing the formation of either of two enantiomeric products by a reaction involving 1,22‐remote intermolecular asymmetric induction.

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Gene duplication in experimental enzyme evolution

Cited by 152 publications

References 14 publications

Physiological Basis of the Selective Advantage of a Spirillum sp. in a Carbon-limited Environment

Physiological Basis of the Selective Advantage of a Spirillum sp. in a Carbon-limited Environment

The cryptic ushA gene (ushA c) in natural isolates of Salmonella enterica (serotype Typhimurium) has been inactivated by a single missense mutation The GenBank accession numbers for the sequences determined in this work are AF188721–AF188732.

Refoldable Foldamers: Global Conformational Switching by Deletion or Insertion of a Single Hydrogen Bond

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