FEBS Letters
Volume 583, Issue 17 , Pages 2727-2733, 3 September 2009

Binding of divalent cations is essential for the activity of the organellar peptidasome in Arabidopsis thaliana, AtPreP

Edited by Miguel De la Rosa

Department of Biochemistry and Biophysics, Stockholm University, SE-106 91 Stockholm, Sweden

Received 3 July 2009; received in revised form 21 July 2009; accepted 22 July 2009. published online 31 July 2009.

Abstract 

The dual-targeted mitochondrial and chloroplastic zinc metallooligopeptidase from Arabidopsis, AtPreP, functions as a peptidasome that degrades targeting peptides and other small unstructured peptides. In addition to Zn located in the catalytic site, AtPreP also contains two Mg-binding sites. We have investigated the role of Mg-binding using AtPreP variants, in which one or both sites were rendered unable to bind Mg2+. Our results show that metal binding besides that of the active site is crucial for AtPreP proteolysis, particularly the inner site appears essential for normal proteolytic function. This is also supported by its evolutionary conservation among all plant species of PreP.

Structured summary

MINT-7231937, MINT-7232017, MINT-7232035, MINT-7232051, MINT-7232070, MINT-7232090:

AtPreP1 (uniprotkb:Q9LJL3) enzymaticly reacts (MI:0414) pF1 beta (uniprotkb:P17614) by protease assay (MI:0435)MINT-7232132:

AtPreP1 (uniprotkb:Q9LJL3) enzymaticly reacts (MI:0414) galanin (uniprotkb:P22466) by protease assay (MI:0435)MINT-7232175:

AtPreP1 (uniprotkb:Q9LJL3) enzymaticly reacts (MI:0414) Cecropin A (uniprotkb:P14954) by protease assay (MI:0435)MINT-7232163:

AtPreP1 (uniprotkb:Q9LJL3) enzymaticly reacts (MI:0414) hPrPss (uniprotkb:P04156) by protease assay (MI:0435)

Keywords: PreP, Protease, Peptidasome, Metal binding, Mitochondria, Chloroplast

To access this article, please choose from the options below

Login to an existing account or Register a new account.

  • Purchase this article for 31.50 USD (You must login/register to purchase this article)

    Online access for 24 hours. The PDF version can be downloaded as your permanent record.

  • Subscribe to this title

    Get unlimited online access to this article and all other articles in this title 24/7 for one year.

  • Claim access now

    For current subscribers with Society Membership or Account Number.

  • Visit SciVerse ScienceDirect to see if you have access via your institution.
 

PII: S0014-5793(09)00588-2

doi:10.1016/j.febslet.2009.07.040

FEBS Letters
Volume 583, Issue 17 , Pages 2727-2733, 3 September 2009

Article Tools

* Image Usage & Resolution