Issue 3, 2017

Not an exception to the rule: the functional significance of intrinsically disordered protein regions in enzymes

Abstract

Intrinsically disordered protein regions (IDPRs) are remarkably common and have unique and important biological functions. Enzymes have long been considered an exception to the rule of protein intrinsic disorder due to the structural requirements for catalysis. Although functionally significant IDPRs have been described in several enzymes, there has been no study quantifying the extent of this phenomenon. We have conducted a multilevel computational analysis of missing regions in X-ray crystal structures in the PDB and predicted disorder in 66 representative proteomes. We found that the fraction of predicted disorder was higher in non-enzymes than enzymes, because non-enzymes were more likely to be fully disordered. However, we also found that transferases, hydrolases and enzymes with multiple assigned functional classifications were similar to non-enzymes in terms of the length of the longest continuous stretch of predicted disorder. Both eukaryotic enzymes and non-enzymes had a greater disorder content than was seen in bacteria. Disorder at the proteome level appears to emerge in response to organismic and functional complexity, and enzymes are not an exception to this rule.

Graphical abstract: Not an exception to the rule: the functional significance of intrinsically disordered protein regions in enzymes

Supplementary files

Article information

Article type
Communication
Submitted
30 Oct 2016
Accepted
12 Jan 2017
First published
12 Jan 2017

Mol. BioSyst., 2017,13, 463-469

Not an exception to the rule: the functional significance of intrinsically disordered protein regions in enzymes

S. DeForte and V. N. Uversky, Mol. BioSyst., 2017, 13, 463 DOI: 10.1039/C6MB00741D

To request permission to reproduce material from this article, please go to the Copyright Clearance Center request page.

If you are an author contributing to an RSC publication, you do not need to request permission provided correct acknowledgement is given.

If you are the author of this article, you do not need to request permission to reproduce figures and diagrams provided correct acknowledgement is given. If you want to reproduce the whole article in a third-party publication (excluding your thesis/dissertation for which permission is not required) please go to the Copyright Clearance Center request page.

Read more about how to correctly acknowledge RSC content.

Spotlight

Advertisements