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A glycosyl hydrolase family 16 gene is responsible for the endogenous production of β-1,3-glucanases within decapod crustaceans

Linton, Stuart M., Cameron, Melissa S., Gray, Michael C., Donald, John A., Saborowski, Reinhard, von Bergen, Martin, Tomm, Janina and Allardyce, Benjamin J. 2015, A glycosyl hydrolase family 16 gene is responsible for the endogenous production of β-1,3-glucanases within decapod crustaceans, Gene, vol. 569, no. 2, pp. 203-217, doi: 10.1016/j.gene.2015.05.056.

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Title A glycosyl hydrolase family 16 gene is responsible for the endogenous production of β-1,3-glucanases within decapod crustaceans
Author(s) Linton, Stuart M.ORCID iD for Linton, Stuart M. orcid.org/0000-0002-8292-7816
Cameron, Melissa S.
Gray, Michael C.
Donald, John A.ORCID iD for Donald, John A. orcid.org/0000-0001-5930-2642
Saborowski, Reinhard
von Bergen, Martin
Tomm, Janina
Allardyce, Benjamin J.ORCID iD for Allardyce, Benjamin J. orcid.org/0000-0003-4009-3371
Journal name Gene
Volume number 569
Issue number 2
Start page 203
End page 217
Total pages 15
Publisher Elsevier
Place of publication Amsterdam, The Netherlands
Publication date 2015-09-15
ISSN 1879-0038
Keyword(s) Cherax destructor
Gecarcoidea natalis
Hemicellulase
Laminarinase
Land crab
β-1,3-glucanase
Summary To identify the gene responsible for the production of a β-1,3-glucanase (laminarinase) within crustacea, a glycosyl hydrolase family 16 (GHF16) gene was sequenced from the midgut glands of the gecarcinid land crab, Gecarcoidea natalis and the freshwater crayfish, Cherax destructor. An open reading frame of 1098bp for G. natalis and 1095bp for C. destructor was sequenced from cDNA. For G. natalis and C. destructor respectively, this encoded putative proteins of 365 and 364 amino acids with molecular masses of 41.4 and 41.5kDa. mRNA for an identical GHF16 protein was also expressed in the haemolymph of C. destructor. These putative proteins contained binding and catalytic domains that are characteristic of a β-1,3-glucanase from glycosyl hydrolase family 16. The amino acid sequences of two short 8-9 amino acid residue peptides from a previously purified β-1,3-glucanase from G. natalis matched exactly that of the putative protein sequence. This plus the molecular masses of the putative proteins matching that of the purified proteins strongly suggests that the sequences obtained encode for a catalytically active β-1,3-glucanase. A glycosyl hydrolase family 16 cDNA was also partially sequenced from the midgut glands of other amphibious (Mictyrisplatycheles and Paragrapsus laevis) and terrestrial decapod species (Coenobita rugosus, Coenobita perlatus, Coenobita brevimanus and Birgus latro) to confirm that the gene is widely expressed within this group. There are three possible hypothesised functions and thus evolutionary routes for the β-1,3-glucanase: 1) a digestive enzyme which hydrolyses β-1,3-glucans, 2) an enzyme which cleaves β-1,3-glycosidic bonds within cell walls to release cell contents or 3) an immune protein which can hydrolyse the cell walls of potentially pathogenic micro-organisms.
Language eng
DOI 10.1016/j.gene.2015.05.056
Field of Research 060303 Biological Adaptation
060309 Phylogeny and Comparative Analysis
060802 Animal Cell and Molecular Biology
Socio Economic Objective 970106 Expanding Knowledge in the Biological Sciences
HERDC Research category C1 Refereed article in a scholarly journal
ERA Research output type C Journal article
Copyright notice ©2015, Elsevier
Persistent URL http://hdl.handle.net/10536/DRO/DU:30074085

Document type: Journal Article
Collection: School of Life and Environmental Sciences
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