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OOP and PreP peptide cleavage products by LC-MS

ABSTRACT: Peptide products from individual cleavage assays with the OOP and PreP1 enzymes were acidified by formic acid and injected into LC-MS. 2012oct12 experiment - sample labels (A1, A2, A3, B1, B2, etc...) condition: 1 - OOP 2 - PreP1 3 - ctrl peptide: A - F1beta H-1 4-15 B - F1beta H-2 43-53 C - F1beta 2-20 D - L29 E - CysD F - SytII G - Mdh oct H - Sdh oct I - P1 J - P22 K - Cox4-preseq L - Abeta28 2013jul12 experiment - sample labels (A11, A21, A31, B11, B21, etc...) condition: 1 - ctrl 2 - OOP 3 - PreP1 peptide: A - thrRS-1 B - thrRS-2 C - F1b-H2 D - L29 E - AT5G36880-11 F - F1b-53 G - AT5G36880-19 H - AT5G36880-26 I - Abeta40

INSTRUMENT(S): LTQ Orbitrap

ORGANISM(S): Arabidopsis Thaliana (mouse-ear Cress)

SUBMITTER: Rui Branca

PROVIDER: PXD000444 | Pride | 2013-09-18

REPOSITORIES: Pride

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Organellar oligopeptidase (OOP) provides a complementary pathway for targeting peptide degradation in mitochondria and chloroplasts.

Kmiec Beata B Teixeira Pedro F PF Berntsson Ronnie P-A RP Murcha Monika W MW Branca Rui M M RM Radomiljac Jordan D JD Regberg Jakob J Svensson Linda M LM Bakali Amin A Langel Ulo U Lehtiö Janne J Whelan James J Stenmark Pål P Glaser Elzbieta E

Proceedings of the National Academy of Sciences of the United States of America 20130916 40

Both mitochondria and chloroplasts contain distinct proteolytic systems for precursor protein processing catalyzed by the mitochondrial and stromal processing peptidases and for the degradation of targeting peptides catalyzed by presequence protease. Here, we have identified and characterized a component of the organellar proteolytic systems in Arabidopsis thaliana, the organellar oligopeptidase, OOP (At5g65620). OOP belongs to the M3A family of peptide-degrading metalloproteases. Using two inde ...[more]

PMID: 24043784

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