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Mechanism of phage P22 tailspike protein folding mutations by Martina Danner; Robert Seckler is a Biochemistry, Genetics and Molecular Biology article available to read on EtoBox.

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## Abstract Temperature‐sensitive folding (__tsf__) and global‐__tsf__‐suppressor (__su__) point mutations affect the folding yields of the trimeric, thermostable phage P22 tailspike endorhamnosidase at elevated temperature, both in vivo and in vitro, but they have little effect on function and stability of the native folded protein. To delineate the mechanism by which these mutations modify the partitioning between productive folding and off‐pathway aggregation, the kinetics of refolding after dilution from acid‐urea solutions and the thermal stability of folding intermediates were analyzed. The study included five __tsf__ mutations of varying severity, the two known __su__ mutations, and four __tsf__/__su__ double mutants. At low temperature (10°C), subunit‐folding rates, measured as an increase in fluorescence, were similar for wild‐type and mutants. At 25°C, however, __tsf__ mutations reduced the rate of subunit folding. The __su__ mutations increased this rate, when present in the __tsf__‐mutant background, but had no effect in the wild‐type background. Conversely, __tsf__ mutations accelerated, and __su__ mutations retarded the irreversible off‐pathway reaction, as revealed b

Who reads Mechanism of phage P22 tailspike protein folding mutations?

Author

Martina Danner; Robert Seckler

Publisher

Cold Spring Harbor Laboratory Press; Wiley (John Wiley & Sons); Wiley-Blackwell; Wiley (ISSN 0961-8368)

Published

1993

Language

EN

Field

Biochemistry, Genetics and Molecular Biology (Life Sciences)