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Current functional metagenomic approaches only expand the existing protease sequence space, but does not presently add any novelty to it

Morris, Laura S. and Marchesi, Julian Roberto 2015. Current functional metagenomic approaches only expand the existing protease sequence space, but does not presently add any novelty to it. Current Microbiology 70 (1) , pp. 19-26. 10.1007/s00284-014-0677-6

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Abstract

Proteases are a fundamental function in many organisms and thus many ecosystems and yet they are rarely obtained in functional metagenomic screens. Here, we have isolated an active protease gene (M1-2; 613 amino acids) which resided in a 38.4 kb fosmid clone that showed a classical protease-positive phenotype. It was classified as a zinc-dependent metalloprotease, with the closest annotated sequence as a neutral protease from Collimonas fungivorans (62 % similarity and 72 % homology). Further characterisation showed that its optimum temperature and pH were 42 °C and 8.0, respectively. Activity was inhibited by EDTA, but inhibition started to be reversed by excess Zn2+. A putative signal peptide was identified bioinformatically and this may be why this protease was successfully isolated using a functional metagenomic screen. Bioinformatic analysis shows that this does not represent a novel protease, but simply expands the current sequence space of known proteases.

Item Type: Article
Date Type: Publication
Status: Published
Schools: Biosciences
Systems Immunity Research Institute (SIURI)
Subjects: Q Science > QR Microbiology
Publisher: Springer Verlag
ISSN: 0343-8651
Last Modified: 08 Mar 2019 16:06
URI: http://orca.cf.ac.uk/id/eprint/71284

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