Homozygous Gly555Glu mutation in the nuclear-encoded 70 kDa flavoprotein gene causes instability of the respiratory chain complex II

A homozygous mutation in the flavoprotein (Fp) gene associated with complex II deficiency was demonstrated in a patient with consanguineous parents. She succumbed at 5½ months of age following a respiratory infection. The c1664G→A transition detected, predicted the substitution of the small uncharge...

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Bibliographic Details
Published in:American journal of medical genetics 2003-07, Vol.120A (1), p.13-18
Main Authors: Van Coster, Rudy, Seneca, S., Smet, J., Van Hecke, R., Gerlo, E., Devreese, B., Van Beeumen, J., Leroy, J.G., De Meirleir, L., Lissens, W.
Format: Article
Language:English
Subjects:
Amino Acids - chemistry
Biological and medical sciences
blue native polyacrylamide gel electrophoresis (Blue Native PAGE)
Cardiomegaly - genetics
Cell Nucleus - metabolism
complex II deficiency
complex instability
Electron Transport - genetics
Electrophoresis, Polyacrylamide Gel
Female
Fibroblasts - metabolism
flavoprotein
Flavoproteins - genetics
Glutamic Acid - genetics
Glutamine - chemistry
Glycine - chemistry
Glycine - genetics
Homozygote
Humans
Infant
Iron - chemistry
iron-containing protein
Medical sciences
Metabolic diseases
Miscellaneous
Models, Molecular
Muscle, Skeletal - metabolism
Mutation
Other metabolic disorders
Oxygen - metabolism
Peptides - chemistry
Phosphorylation
Protein Structure, Tertiary
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Description
Summary:A homozygous mutation in the flavoprotein (Fp) gene associated with complex II deficiency was demonstrated in a patient with consanguineous parents. She succumbed at 5½ months of age following a respiratory infection. The c1664G→A transition detected, predicted the substitution of the small uncharged glycine at position 555 by glutamic acid. Her clinical course was at variance with the Leigh syndrome in three previously reported patients due to Fp gene mutations. In this proband, CRM for flavoprotein as well as iron‐containing protein (Ip) was decreased, CRM for the entire complex II (130 kDa) being reduced even more. This observation prompts speculation of a labile interaction between Ip and Fp polypeptides and of a key role of the amino acid at position 555 in the interacting domain. © 2003 Wiley‐Liss, Inc.
ISSN:1552-4825
0148-7299
1552-4833
1096-8628
DOI:10.1002/ajmg.a.10202