The GLRX5 gene contains 2
exons and encodes for a protein that is 13 kDa in size. The protein is highly expressed in
erythroid cells.[7]Crystal structure of the GLRX5 protein reveals that the protein likely exists as a tetramer with two
Fe-S clusters buried in the interior.[8]
Function
GLRX5 is a
mitochondrial protein is conserved evolutionarily and plays a role in the formation of
iron-sulfur clusters, which function to maintain
iron homeostasis within the mitochondria and in the cell. GLRX5 is required for the steps in
haem synthesis that involves mitochondrial enzymes,[9] and is therefore involved in
hematopoiesis. GLRX5 activity is required for normal regulation of hemoglobin synthesis by the iron-sulfur protein
ACO1. The function of GLRX5 is highly conserved evolutionarily.[10]
Clinical significance
Mutations in the GLRX5 gene have been associated with
sideroblastic anemia,[11] variant
glycine encephalopathy (also known as non-ketotic hyperglycinemia,
NKH).[12] as well as pyridoxine-refractory, autosomal recessive anemia (PRARSA).[10] Cells with mutations in GLRX5 activity show deficiency in Fe-S cluster synthesis, which is likely causative of the observed symptoms.[7]
The GLRX5 gene contains 2
exons and encodes for a protein that is 13 kDa in size. The protein is highly expressed in
erythroid cells.[7]Crystal structure of the GLRX5 protein reveals that the protein likely exists as a tetramer with two
Fe-S clusters buried in the interior.[8]
Function
GLRX5 is a
mitochondrial protein is conserved evolutionarily and plays a role in the formation of
iron-sulfur clusters, which function to maintain
iron homeostasis within the mitochondria and in the cell. GLRX5 is required for the steps in
haem synthesis that involves mitochondrial enzymes,[9] and is therefore involved in
hematopoiesis. GLRX5 activity is required for normal regulation of hemoglobin synthesis by the iron-sulfur protein
ACO1. The function of GLRX5 is highly conserved evolutionarily.[10]
Clinical significance
Mutations in the GLRX5 gene have been associated with
sideroblastic anemia,[11] variant
glycine encephalopathy (also known as non-ketotic hyperglycinemia,
NKH).[12] as well as pyridoxine-refractory, autosomal recessive anemia (PRARSA).[10] Cells with mutations in GLRX5 activity show deficiency in Fe-S cluster synthesis, which is likely causative of the observed symptoms.[7]