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The FASEB Journal, Vol 10, 153-158, Copyright © 1996 by The Federation of American Societies for Experimental Biology

RESEARCH COMMUNICATIONS

Unproductive folding of the human G6PD-deficient variant A-

F Gomez-Gallego, A Garrido-Pertierra, PJ Mason and JM Bautista
Departamento di Bioquimica y Biologia Molecular IV, Universidad Complutense de Madrid, Facultad de Veterinaria, Ciudad Universitaria, Spain.

Human glucose-6-phosphate dehydrogenase (G6PD) deficiency almost invariably results from the presence of missense mutations in the X- linked gene encoding G6PD. The common African deficient variant G6PD A- differs from the normal G6PD B by two amino acid substitutions. Only one of these mutations is found on its own, resulting in the nondeficient variant G6PD A. Deficiency is always associated with decreased G6PD activity in red cells, leading to a variety of clinical manifestations. A group of deficient variants, including A-, have near- normal affinity for the substrates G6P and NADP. In these cases, deficiency is caused by a decreased number of catalytically active molecules per cell due to intracellular instability of the mutated G6PD, although the mechanism for this in vivo instability is unknown. Here we report that in vitro folding of the A- variant mainly renders partially folded polypeptides that do not undergo the dimerization required for activity. Under the same conditions, the nondeficient variants B and A undergo folding to produce active dimers with normal mobilities in native gels and normal kinetic properties. The loss of intrinsic folding determinants in the A- variant may underlie the mechanism of its in vivo instability.


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Copyright © 1996 by The Federation of American Societies for Experimental Biology.