Abstract:
:The tailspike protein (TSP) of bacteriophage P22 is a homotrimeric multifunctional protein responsible for cell attachment and hydrolysis of the Salmonella typhimurium host cell receptor. Despite the folding of TSP involves the formation of thermolabile intermediates, the mature protein is extremely resistant to heat and detergent denaturation. We have analyzed the thermal resistance and unfolding pathway of two mutant, functional TSPs carrying end-terminal peptide fusions. Whereas the C-terminal fusion has minor effects on the TSP stability, the presence of a 23-mer foreign peptide at the N terminus (protein ATSP) results in a significant enhancement of the thermal resistance by retarding the first transition step of the unfolding process. At 65 degrees C and in 2% SDS, the unfolding rate constant for the transition from the native to the unfolding intermediate is 9.3 x 10(-4) s(-1) for ATSP versus 1.7 x 10(-3) s(-1) for wild-type TSP. On the other hand, the electrophoretic mobility of ATSP intermediates is greatly affected, proving structural modifications induced by the fused peptide. These results suggest a critical participation of the N-terminal domain in the unfolding kinetic barriers generated during the TSP denaturation pathway.
journal_name
FEBS Lettjournal_title
FEBS lettersauthors
Carbonell X,Villaverde Adoi
10.1016/s0014-5793(98)00876-xsubject
Has Abstractpub_date
1998-08-07 00:00:00pages
228-30issue
3eissn
0014-5793issn
1873-3468pii
S0014-5793(98)00876-Xjournal_volume
432pub_type
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