The stability and hydrophobicity of cytosolic and mitochondrial malate dehydrogenases and their relation to chaperonin‐assisted folding

FEBS Letters

Atkinson, Tony³  Clarke, Anthony R.²  Burston, Steven G.²  Cortés, Antonio¹  Holbrook, J.John²  Staniforth, Rosemary A.² 

[1] Department of Biochemistry and Physiology, University of Barcelona, Marti y Franquès 1, 08028 Barcelona, Spain;Department of Biochemistry and Molecular Recognition Centre, University of Bristol, School of Medical Sciences, University Walk, Bristol, BS8, 1TD, UK;Microbial Technology Laboratory, Public Health Laboratory Service, Centre for Applied Microbiology and Research, Salisbury, Wiltshire, SP4 OJG, UK

关键词: Chaperonin;    Protein folding;    Malate dehydrogenase;    mMDH;    mitochondrial malate dehydrogenase;    cMDH;    cytosolic malate dehydrogenase;    GdmCl;    guanidinium chloride;    cpn60;    chaperonin 60;    cpn10;    chaperonin 10;    Pi;    orthophosphate;   

DOI  :  10.1016/0014-5793(94)00348-3

学科分类：生物化学/生物物理

来源: John Wiley & Sons Ltd.

【 摘 要 】

mMDH and cMDH are structurally homologous enzymes which show very different responses to chaperonins during folding. The hydrophilic and stable cMDH is bound by cpn60 but released by MG-ATP alone, while the hydrophobic and unstable mMDH requires both Mg-ATP and cpn 10. Citrate equalises the stability of the native state of the two proteins but has no effect on the co-chaperonin requirement, implying that hydrophobicity, and not stability, is the determining factor. The yield and rate of folding of cMDH is unaffected while that of mMDH is markedly increased by the presence of cpn60, cpn10 and Mg-ATP. In 200 mM orthophosphate, chaperonins do not enhance the rate of folding of mMDH, but in low phosphate concentrations chaperonin-assisted folding is 3–4-times faster.

【 授权许可】

Unknown