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Structure-function analysis of a broad specificity Populus trichocarpa endo-β-glucanase reveals an evolutionary link between bacterial licheninases and plant XTH gene products

Eklöf, Jens M. (författare)
KTH,Glykovetenskap
Shojania, S. (författare)
Okon, M. (författare)
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McIntosh, L. P. (författare)
Brumer, Harry (författare)
KTH,Glykovetenskap
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 (creator_code:org_t)
2013
2013
Engelska.
Ingår i: Journal of Biological Chemistry. - 0021-9258 .- 1083-351X. ; 288:22, s. 15786-15799
  • Tidskriftsartikel (refereegranskat)
Abstract Ämnesord
Stäng  
  • The large xyloglucan endotransglycosylase/hydrolase (XTH) gene family continues to be the focus of much attention in studies of plant cell wall morphogenesis due to the unique catalytic functions of the enzymes it encodes. The XTH gene products compose a subfamily of glycoside hydrolase family 16 (GH16), which also comprises a broad range of microbial endoglucanases and endogalactanases, as well as yeast cell wall chitin/β-glucan transglycosylases. Previous whole-family phylogenetic analyses have suggested that the closest relatives to the XTH gene products are the bacterial licheninases (EC 3.2.1.73), which specifically hydrolyze linear mixed linkage β(1→3)/β(1→4)-glucans. In addition to their specificity for the highly branched xyloglucan polysaccharide, XTH gene products are distinguished from the licheninases and other GH16 enzyme subfamilies by significant active site loop alterations and a large C-terminal extension. Given these differences, the molecular evolution of the XTH gene products in GH16 has remained enigmatic. Here, we present the biochemical and structural analysis of a unique, mixed function endoglucanase from black cottonwood (Populus trichocarpa), which reveals a small, newly recognized subfamily of GH16 members intermediate between the bacterial licheninases and plant XTH gene products. We postulate that this clade comprises an important link in the evolution of the large plant XTH gene families from a putative microbial ancestor. As such, this analysis provides new insights into the diversification of GH16 and further unites the apparently disparate members of this important family of proteins.

Ämnesord

NATURVETENSKAP  -- Biologi -- Biokemi och molekylärbiologi (hsv//swe)
NATURAL SCIENCES  -- Biological Sciences -- Biochemistry and Molecular Biology (hsv//eng)

Nyckelord

Broad specificities
C-terminal extensions
Catalytic functions
Glycoside hydrolase family 16
Molecular evolution
Phylogenetic analysis
Populus trichocarpa
Structure-function analysis
Catalysis
Enzyme activity
Molecular biology
Plant cell culture
Plants (botany)
Polymers
Genes
bacterial enzyme
endo beta glucanase
glucan synthase
licheninase
unclassified drug
article
cladistics
enzyme specificity
enzyme structure
multigene family
nucleotide sequence
plant gene
priority journal
structure activity relation
XTH gene
Carbohydrate Processing
Cellulase
Enzyme Kinetics
Glycoside Hydrolases
Plant Cell Wall
Polysaccharide
Xyloglucan
Xyloglucan Endotransglycosylase/Hydrolase (XTH)
Bacterial Proteins
Catalytic Domain
Evolution
Molecular
Glycosyltransferases
Phylogeny
Plant Proteins
Populus
Protein Structure
Secondary

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