dc.contributor.author |
Bellí i Martínez, Gemma |
dc.contributor.author |
Polaina, Julio |
dc.contributor.author |
Tamarit Sumalla, Jordi |
dc.contributor.author |
Torre Ruiz, M. A. de la |
dc.contributor.author |
Rodríguez Manzanaque, Maria Teresa |
dc.contributor.author |
Ros Salvador, Joaquim |
dc.contributor.author |
Herrero Perpiñán, Enrique |
dc.date |
2015-07-07T10:20:56Z |
dc.date |
2002 |
dc.identifier |
0021-9258 |
dc.identifier |
http://hdl.handle.net/10459.1/48416 |
dc.identifier |
https://doi.org/10.1074/jbc.M201688200 |
dc.identifier.uri |
http://hdl.handle.net/10459.1/48416 |
dc.description |
Grx5 defines a family of yeast monothiol glutaredox-
ins that also includes Grx3 and Grx4. All three proteins
display significant sequence homology with proteins
found from bacteria to humans. Grx5 is involved in iron/
sulfur cluster assembly at the mitochondria, but the
function of Grx3 and Grx4 is unknown. Three-dimen-
sional modeling based on known dithiol glutaredoxin
structures predicted a thioredoxin fold structure for
Grx5. Positionally conserved amino acids in this glu-
taredoxin family were replaced in Grx5, and the effect
on the biological function of the protein has been tested.
For all changes studied, there was a correlation between
the effects on several different phenotypes: sensitivity
to oxidants, constitutive protein oxidation, ability for
respiratory growth, auxotrophy for a number of amino
acids, and iron accumulation. Cys60 and Gly61 are essen-
tial for Grx5 function, whereas other single or double
substitutions in the same region had no phenotypic ef-
fects. Gly115 and Gly116 could be important for the for-
mation of a glutathione cleft on the Grx5 surface, in
contrast to adjacent Cys117. Substitution of Phe50 alters
the -sheet in the thioredoxin fold structure and inhib-
its Grx5 function. None of the substitutions tested affect
the structure at a significant enough level to reduce
protein stability. |
dc.language |
eng |
dc.publisher |
The American Society for Biochemistry and Molecular Biology |
dc.relation |
Reproducció del document publicat a https://doi.org/10.1074/jbc.M201688200 |
dc.relation |
The Journal of Biological Chemistry, 2002, vol. 277, núm 40, p. 37590-37596 |
dc.rights |
(c) The American Society for Biochemistry and Molecular Biology, 2002 |
dc.rights |
info:eu-repo/semantics/openAccess |
dc.title |
Structure-function analysis of yeast Grx5 monothiol glutaredoxin defines essential amino acids for the function of the protein |
dc.type |
article |
dc.type |
publishedVersion |