Article ID | Journal | Published Year | Pages | File Type |
---|---|---|---|---|
2050381 | FEBS Letters | 2009 | 7 Pages |
Abstract
We report that Pro74 in human stefin B is critical for fibril formation and that proline isomerization plays an important role. The stefin B P74S mutant did not fibrillate over the time of observation at 25 °C, and it exhibited a prolonged lag phase at 30 °C and 37 °C. The peptidyl prolyl cis/trans isomerase cyclophilin A, when added to the wild-type protein, exerted two effects: it prolonged the lag phase and increased the yield and length of the fibrils. Addition of the inactive cyclophilin A R55A variant still resulted in a prolonged lag phase but did not mediate the increase of the final fibril yield. These results demonstrate that peptidyl prolyl cis/trans isomerism is rate-limiting in stefin B fibril formation.
Keywords
Related Topics
Life Sciences
Agricultural and Biological Sciences
Plant Science
Authors
Aida Smajlović, Selma Berbić, Cordelia Schiene-Fischer, Magda Tušek-Žnidarič, Ajda Taler, Saša Jenko-Kokalj, Dušan Turk, Eva Žerovnik,