National Academy of Sciences;United States: National Academy of Sciences
摘要:
摘要： Kinesins perform mechanical work to power a variety of cellular functions, from mitosis to organelle transport. Distinct functions shape distinct enzymologies, and this is illustrated by comparing kinesin-1, a highly processive transport motor that can work alone, to Eg5, a minimally processive mitotic motor that works in large ensembles. Although crystallographic models for both motors reveal similar structures for the domains involved in mechanochemical transduction—including switch-1 and the neck linker—how movement of these two domains is coordinated through the ATPase cycle remains unknown. We have addressed this issue by using a novel combination of transient kinetics and time-resolved fluorescence, which we refer to as “structural kinetics,” to map the timing of structural changes in the switch-1 loop and neck linker. We find that differences between the structural kinetics of Eg5 and kinesin-1 yield insights into how these two motors adapt their enzymologies for their distinct functions. 其他題名： Proc Natl Acad Sci USA 其他題名： Proc Natl Acad Sci U S A 出版者： United States: National Academy of Sciences 出版日期： 2015-12-01 出處： Proceedings of the National Academy of Sciences - PNAS, 2015-12, Vol.112 (48), p.E6606-E6613 資源來源： JSTOR 版權： Volumes 1–89 and 106–112, copyright as a collective work only; author(s) retains copyright to individual articles 版權： Copyright National Academy of Sciences Dec 1, 2015 識別號： ISSN: 0027-8424 識別號： ISSN: 1091-6490 識別號： EISSN: 1091-6490 識別號： DOI: 10.1073/pnas.1512305112 識別號： PMID: 26627252
