Protein Engineering, Vol 11, 329-332, Copyright © 1998 by Oxford University Press
KA Miroshnikov, EI Marusich, ME Cerritelli, N Cheng, CC Hyde, AC Steven and VV Mesyanzhinov
The adsorption specificity of bacteriophage T4 is determined by genes 12
and 37, encoding the short tail-fibers (STF) and the distal part of the
long tail-fibers (LTF), respectively. Both are trimeric proteins with rod
domains made up of similar tandem quasi-repeats, approximately 40 amino
acids long. Their assembly requires the viral chaperones gp57A and gp38.
Here we report that fusing fragments of gp12 and gp37 to another trimeric
T4 fibrous protein, fibritin, facilitates correct assembly, thereby
by-passing the chaperone requirement. Fibritin is an alpha-helical coiled
coil protein whose C-terminal part (fibritin E, comprising the last 120
residues) has recently been solved to atomic resolution. Gp12 fragments of
109 and 70 amino acids, corresponding to three and two quasi-repeats
respectively, were fused to the C-terminus of fibritin E. A similar chimera
was designed for the last 63 residues of gp37, which contain four copies of
the pentapeptide Gly-X-His-X-His and assume a narrow rigid structure in the
LTF distal tip. Expressed from plasmids, all three chimeras form soluble
trimers that are resistant to dissociation by SDS and digestion by trypsin,
indicative of correct folding and oligomerization.
ARTICLES
Engineering trimeric fibrous proteins based on bacteriophage T4 adhesins
Howard Hughes Medical Institute, Bach Institute of Biochemistry, Moscow, Russia.
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