Flavinylation and assembly of succinate dehydrogenase are dependent on the C-terminal tail of the flavoprotein subunit.

ABSTRACT:

Background

Succinate dehydrogenase (SDH) requires a covalent addition of FAD for catalytic function.

Results

Mutational analyses of Sdh1 implicate C-terminal region Arg residues involvement in covalent flavinylation and SDH assembly.

Conclusion

SDH assembly is dependent on FAD binding to Sdh1 but not covalent binding.

Significance

These results document the basis for the SDH deficiency and pathology seen with mutations in human Sdh1. The enzymatic function of succinate dehydrogenase (SDH) is dependent on covalent attachment of FAD on the ~70-kDa flavoprotein subunit Sdh1. We show presently that flavinylation of the Sdh1 subunit of succinate dehydrogenase is dependent on a set of two spatially close C-terminal arginine residues that are distant from the FAD bind

SUBMITTER: Kim HJ 

PROVIDER: S-EPMC3504780 | biostudies-literature | 2012 Nov

REPOSITORIES: biostudies-literature