NDLI: Phage P22 tailspike protein: removal of head-binding domain unmasks effects of folding mutations on native-state thermal stability.

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Phage P22 tailspike protein: removal of head-binding domain unmasks effects of folding mutations on native-state thermal stability.

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Phage P22 tailspike protein: removal of head-binding domain unmasks effects of folding mutations on native-state thermal stability.

Content Provider	World Health Organization (WHO)-Global Index Medicus
Author	Miller, S. Schuler, B. Seckler, R.
Description	Country affiliation: Germany Author Affiliation: Miller S ( Institut für Biophysik und Physikalische Biochemie, Universität Regensburg, Germany.)
Abstract	A shortened, recombinant protein comprising residues 109-666 of the tailspike endorhamnosidase of Salmonella phage P22 was purified from Escherichia coli and crystallized. Like the full-length tailspike, the protein lacking the amino-terminal head-binding domain is an SDS-resistant, thermostable trimer. Its fluorescence and circular dichroism spectra indicate native structure. Oligosaccharide binding and endoglycosidase activities of both proteins are identical. A number of tailspike folding mutants have been obtained previously in a genetic approach to protein folding. Two temperature-sensitive-folding (tsf) mutations and the four known global second-site suppressor (su) mutations were introduced into the shortened protein and found to reduce or increase folding yields at high temperature. The mutational effects on folding yields and subunit folding kinetics parallel those observed with the full-length protein. They mirror the in vivo phenotypes and are consistent with the substitutions altering the stability of thermolabile folding intermediates. Because full-length and shortened tailspikes aggregate upon thermal denaturation, and their denaturant-induced unfolding displays hysteresis, kinetics of thermal unfolding were measured to assess the stability of the native proteins. Unfolding of the shortened wild-type protein in the presence of 2% SDS at 71 degrees C occurs at a rate of 9.2 x 10(-4) s(-1). It reflects the second kinetic phase of unfolding of the full-length protein. All six mutations were found to affect the thermal stability of the native protein. Both tsf mutations accelerate thermal unfolding about 10-fold. Two of the su mutations retard thermal unfolding up to 5-fold, while the remaining two mutations accelerate unfolding up to 5-fold. The mutational effects can be rationalized on the background of the recently determined crystal structure of the protein.
ISSN	09618368
e-ISSN	1469896X
Journal	Protein Science
Issue Number	10
Volume Number	7
Language	English
Publisher	Wiley-Blackwell (on behalf of The Protein Society)
Publisher Date	1998-10-01
Publisher Place	United States
Access Restriction	Open
Subject Keyword	Bacteriophage P22 Enzymology Enzyme Stability Genetics Glycoside Hydrolases Chemistry Protein Denaturation Viral Tail Proteins Fluorescence Kinetics Models, Molecular Mutagenesis, Site-directed Protein Conformation Protein Folding Recombinant Proteins Salmonella Virology Temperature Tryptophan Research Support, Non-u.s. Gov't Discipline Biochemistry
Content Type	Text
Resource Type	Article
Subject	Medicine Molecular Biology Biochemistry

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