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Open AccessArticle

Novel Insights from Comparative In Silico Analysis of Green Microalgal Cellulases

1
Environmental Research and Innovation (ERIN) Department, Luxembourg Institute of Science and Technology (LIST), 5 Avenue des Hauts-Fourneaux, L-4362 Esch/Alzette, Luxembourg
2
Life Sciences Department, King Fahd University of Petroleum and Minerals (KFUPM), Dhahran 31261, Saudi Arabia
*
Authors to whom correspondence should be addressed.
Int. J. Mol. Sci. 2018, 19(6), 1782; https://doi.org/10.3390/ijms19061782
Received: 10 May 2018 / Revised: 8 June 2018 / Accepted: 8 June 2018 / Published: 15 June 2018
(This article belongs to the Special Issue Plant Cell Wall Proteins and Development)
The assumption that cellulose degradation and assimilation can only be carried out by heterotrophic organisms was shattered in 2012 when it was discovered that the unicellular green alga, Chlamydomonas reinhardtii (Cr), can utilize cellulose for growth under CO2-limiting conditions. Publications of genomes/transcriptomes of the colonial microalgae, Gonium pectorale (Gp) and Volvox carteri (Vc), between 2010–2016 prompted us to look for cellulase genes in these algae and to compare them to cellulases from bacteria, fungi, lower/higher plants, and invertebrate metazoans. Interestingly, algal catalytic domains (CDs), belonging to the family GH9, clustered separately and showed the highest (33–42%) and lowest (17–36%) sequence identity with respect to cellulases from invertebrate metazoans and bacteria, respectively, whereas the identity with cellulases from plants was only 27–33%. Based on comparative multiple alignments and homology models, the domain arrangement and active-site architecture of algal cellulases are described in detail. It was found that all algal cellulases are modular, consisting of putative novel cysteine-rich carbohydrate-binding modules (CBMs) and proline/serine-(PS) rich linkers. Two genes were found to encode a protein with a putative Ig-like domain and a cellulase with an unknown domain, respectively. A feature observed in one cellulase homolog from Gp and shared by a spinach cellulase is the existence of two CDs separated by linkers and with a C-terminal CBM. Dockerin and Fn-3-like domains, typically found in bacterial cellulases, are absent in algal enzymes. The targeted gene expression analysis shows that two Gp cellulases consisting, respectively, of a single and two CDs were upregulated upon filter paper addition to the medium. View Full-Text
Keywords: cellulase; glycosyl hydrolase family 9; carbohydrate binding module (CBM); bioinformatics; RT-qPCR cellulase; glycosyl hydrolase family 9; carbohydrate binding module (CBM); bioinformatics; RT-qPCR
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MDPI and ACS Style

Guerriero, G.; Sergeant, K.; Legay, S.; Hausman, J.-F.; Cauchie, H.-M.; Ahmad, I.; Siddiqui, K.S. Novel Insights from Comparative In Silico Analysis of Green Microalgal Cellulases. Int. J. Mol. Sci. 2018, 19, 1782.

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