Molecular evolution of plant beta-glucan endohydrolases.
The evolutionary relationships of two classes of plant beta-glucan endohydrolases have been examined by comparison of their substrate specificities, their three-dimensional conformations and the structural features of their corresponding genes. These comparative studies provide compelling evidence that the (1-->3)-beta-glucanases and (1-->3,1-->4)-beta-glucanases from higher plants share a common ancestry and, in all likelihood, that the (1-->3,1-->4)-beta-glucanases diverged from the (1-->3)-beta-glucanases during the appearance of the graminaceous monocotyledons. The evolution of (1-->3,1-->4)-beta-glucanases from (1-->3)-beta-glucanases does not appear to have invoked 'modular' mechanisms of change, such as those caused by exon shuffling or recombination. Instead, the shift in specificity has been acquired through a limited number of point mutations that have resulted in amino acid substitutions along the substrate-binding cleft. This is consistent with current theories that the evolution of new enzymic activity is often achieved through duplication of the gene encoding an existing enzyme which is capable of performing the required chemistry, in this case the hydrolysis of a glycosidic linkage, followed by the mutational alteration and fine-tuning of substrate specificity. The evolution of a new specificity has enabled a dramatic shift in the functional capabilities of the enzymes. (1-->3)-beta-Glucanases that play a major role, inter alia, in the protection of the plant against pathogenic microorganisms through their ability to hydrolyse the (1-->3)-beta-glucans of fungal cell walls, appear to have been recruited to generate (1-->3,1-->4)-beta-glucanases, which quite specifically hydrolyse plant cell wall (1-->3,1-->4)-beta-glucans in the graminaceous monocotyledons during normal wall metabolism. Thus, one class of beta-glucan endohydrolase can degrade beta-glucans in fungal walls, while the other hydrolyses structurally distinct beta-glucans of plant cell walls. Detailed information on the three-dimensional structures of the enzymes and the identification of catalytic amino acids now present opportunities to explore the precise molecular and atomic details of substrate-binding, catalytic mechanisms and the sequence of molecular events that resulted in the evolution of the substrate specificities of the two classes of enzyme.
Høj
P B
PB
Department of Horticulture, Viticulture and Oenology, University of Adelaide, Glen Osmond, South Australia.
Fincher
G B
GB
D000595:Amino Acid Sequence; D001665:Binding Sites / Q000235:genetics; D005075:Biological Evolution; D002240:Carbohydrate Sequence; D002480:Cellulase / Q000737:chemistry / Q000235:genetics / Q000378:metabolism; D044644:Endo-1,3(4)-beta-Glucanase; D005936:Glucans / Q000737:chemistry; D006026:Glycoside Hydrolases / Q000737:chemistry / Q000235:genetics* / Q000378:metabolism; D008958:Models, Molecular; D008969:Molecular Sequence Data; D010802:Phylogeny; D010944:Plants / Q000201:enzymology* / Q000235:genetics*; D012641:Selection, Genetic; D013379:Substrate Specificity
D005936:Glucans; D006026:Glycoside Hydrolases; D002480:Cellulase; D044644:Endo-1,3(4)-beta-Glucanase; C028020:licheninase