Role of heat-shock proteins and cobalamine in maintaining methionine synthase activity.

Michał Grabowski; Rafał Banasiuk; Alicja Węgrzyn; Barbara Kędzierska; Jan Lica; Zyta Banecka-Majkutewicz; Bogdan Banecki

doi:10.18388/abp.2012_2082

Role of heat-shock proteins and cobalamine in maintaining methionine synthase activity.

Michał Grabowski Department of Molecular and Cellular Biology, Intercollegiate Faculty of Biotechnology University of Gdańsk and Medical University of Gdańsk, Poland.;
Rafał Banasiuk
Alicja Węgrzyn
Barbara Kędzierska
Jan Lica
Zyta Banecka-Majkutewicz
Bogdan Banecki

DOI: https://doi.org/10.18388/abp.2012_2082

Abstract

Atheromatous plaque is one of the most common cardiovascular-related diseases. Reports show a connection between its development and the levels of homocysteine. In pathological states high levels of homocysteine in the organism can be caused by the malfunction of the methionine synthase pathway. Bacterial methionine synthase (MetH) is a homologue of the human methionine syntase (MS). In this study we aimed to investigate the functional relations between MetH and its cofactor--cobalamine--under stress conditions. We have demonstrated that heat shock proteins (Hsp 70/100 system or HtpG) can protect MetH activity under stress conditions. Moreover, in the presence of cobalamine they can restore the activity of partially denatured methionine synthase.

Published

2012-12-18

Issue

Vol. 59 No. 4 (2012)

Section

Articles

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