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 ORCID: https://orcid.org/0000-0002-7994-5239 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:	28 Oct 2022 08:34
URI:	https://orca.cardiff.ac.uk/id/eprint/71284

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