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Proteomics Insights

Synopsis: An open access, peer reviewed electronic journal that covers proteomics.


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About this journal

ISSN: 1178-6418



Aims and scope:

Proteomics Insights is a peer-reviewed, open access journal which covers the rapidly expanding field of proteomics. Proteomics is an increasingly important part of studying and understanding organisms and this journal acts as a forum for these findings.

Proteomics Insights welcomes articles from all areas of proteomics including whole proteome analysis, protein expression profiling, disease, and analysis of cellular systems, organelles and protein complexes in terms of structure, function, properties and interactions. Papers on related methodology, software, databases, technology and applications are also welcome.

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  • OAIster

Editorial standards and procedures:

Submissions, excluding editorials, letters to the editor and dedications, will be peer reviewed by two reviewers.  Reviewers are required to provide fair, balanced and constructive reports.  

Under our Fairness in Peer Review Policy authors may appeal against reviewers' recommendations which are ill-founded, unobjective or unfair.  Appeals are considered by the Editor in Chief or Associate Editor.

Papers are not sent to peer reviewers following submission of a revised manuscript. Editorial decisions on re-submitted papers are based on the author's response to the initial peer review report.

National Institutes of Health Public Access Policy compliant:

As of April 7 2008, the US NIH Public Access Policy requires that all peer reviewed articles resulting from research carried out with NIH funding be deposited in the Pubmed Central archive.

If you are an NIH employee or grantee Libertas Academica will ensure that you comply with the policy by depositing your paper at Pubmed Central on your behalf. 



 
 
 


Oxidation of an Adjacent Methionine Residue Inhibits Regulatory Seryl-Phosphorylation of Pyruvate Dehydrogenase

Authors: Jan A. Miernyk, Mark L. Johnston, Steve C. Huber, Alejandro Tovar-Méndez, Elizabeth Hoyos and Douglas D. Randall
Publication Date: 22 Jul 2009
Proteomics Insights 2009:2 15-22

Jan A. Miernyk1,2,3, Mark L. Johnston1, Steve C. Huber4,5, Alejandro Tovar-Méndez2, Elizabeth Hoyos2 and Douglas D. Randall2,3

1Plant Genetics Research Unit, USDA, Agricultural Research Service, 108 Curtis Hall, University of Missouri, Columbia, MO 65211. 2Department of Biochemistry, University of Missouri, Columbia, MO 65211. 3Interdisciplinary Plant Group, University of Missouri, Columbia, MO. 4Photosynthesis Research Unit, USDA, Agricultural Research Service, 197 ERML, University of Illinois, Urbana, IL 61801. 5Department of Plant Biology and Crop Sciences, University of Illinois, Urbana, IL 61801.

Abstract

A Met residue is located adjacent to phosphorylation site 1 in the sequences of mitochondrial pyruvate dehydrogenase E1α subunits. When synthetic peptides including site 1 were treated with H2O2, the Met residue was oxidized to methionine sulfoxide (MetSO), and the peptides were no longer phosphorylated by E1α-kinase. Isolated mitochondria were incubated under state III or IV conditions, lysed, the pyruvate dehydrogenase complex (PDC) immunoprecipitated, and tryptic peptides analyzed by MALDI-TOF mass spectrometry. In all instances both Met and MetSO site 1 tryptic-peptides were detected. Similar results were obtained when suspension-cultured cells were incubated with chemical agents known to stimulate production of reactive oxygen species within the mitochondria. Treatment with these agents had no effect upon the amount of total PDC, but decreased the proportion of P-PDC. We propose that the redox-state of the Met residue adjacent to phosphorylation site 1 of pyruvate dehydrogenase contributes to overall regulation of PDC activity in vivo.

Categories: Proteomics


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