Campus Units

Genetics, Development and Cell Biology, Plant Pathology and Microbiology

Document Type

Article

Publication Version

Published Version

Publication Date

2-2016

Journal or Book Title

Journal of Experimental Botany

Volume

67

Issue

8

First Page

2339

Last Page

2351

DOI

10.1093/jxb/erw044

Abstract

Proteolytic processing of secretory proteins to yield an active form generally involves specific proteolytic cleavage of a pre-protein. Multiple specific proteases have been identified that target specific pre-protein processing sites in animals. However, characterization of site-specific proteolysis of plant pre-proteins is still evolving. In this study, we characterized proteolytic processing of Chlamydomonas periplasmic carbonic anhydrase 1 (CAH1) in Arabidopsis. CAH1 pre-protein undergoes extensive post-translational modification in the endomembrane system, including glycosylation, disulfide bond formation and proteolytic removal of a peptide ‘spacer’ region, resulting in a mature, heterotetrameric enzyme with two large and two small subunits. We generated a series of small-scale and large-scale modifications to the spacer and flanking regions to identify potential protease target motifs. Surprisingly, we found that the endoproteolytic removal of the spacer from the CAH1 pre-protein proceeded via an opportunistic process apparently followed by further maturation via amino and carboxy peptidases. We also discovered that the spacer itself is not required for processing, which appears to be dependent only on the number of amino acids separating two key disulfide-bond-forming cysteines. Our data suggest a novel, opportunistic route for pre-protein processing of CAH1.

Comments

The article is published as Juvale, P, R Wagner, MH Spalding 2016 Novel processing of the Chlamydomonas periplasmic carbonic anhydrase in Arabidopsis. Journal of Experimental Botany 67:2339-2351 (doi: 10.1093/jxb/erw044). 10.1093/jxb/erw044. Posted with permission.

Creative Commons License

Creative Commons Attribution 4.0 License
This work is licensed under a Creative Commons Attribution 4.0 License.

Copyright Owner

The Authors

Language

en

File Format

application/pdf

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