Comparison of folding rates of homologous prokaryotic and eukaryotic proteins.
J Biol Chem
; 275(25): 18619-22, 2000 Jun 23.
Article
en En
| MEDLINE
| ID: mdl-10781576
ABSTRACT
The rate of polypeptide chain elongation is up to one order of magnitude faster in prokaryotic cells than in eukaryotes. Here we report that the rates of in vitro refolding of orthologous prokaryotic and eukaryotic proteins correlate with their differential rates of biosynthesis. The mitochondrial and cytosolic aspartate aminotransferases of chicken and aspartate aminotransferase of Escherichia coli show pairwise sequence identities of 41-48% and nearly identical three-dimensional structures. Nevertheless, the prokaryotic enzyme refolded 6 times faster (at 25 degrees C) than the eukaryotic isoenzymes after denaturation in 6 m guanidine hydrochloride. Prokaryotic malate dehydrogenase and lactate dehydrogenase also renatured faster than their orthologous eukaryotic counterparts, suggesting that evolutionary pressure has adapted the rate of folding to the rate of elongation of polypeptide chains.
Buscar en Google
Base de datos:
MEDLINE
Asunto principal:
Aspartato Aminotransferasas
/
Proteínas Bacterianas
/
Escherichia coli
Idioma:
En
Revista:
J Biol Chem
Año:
2000
Tipo del documento:
Article