Ontology highlight
ABSTRACT:
SUBMITTER: Krementsova EB
PROVIDER: S-EPMC3257522 | biostudies-literature | 2011 Nov
REPOSITORIES: biostudies-literature
Krementsova Elena B EB Hodges Alex R AR Bookwalter Carol S CS Sladewski Thomas E TE Travaglia Mirko M Sweeney H Lee HL Trybus Kathleen M KM
The Journal of cell biology 20111101 4
Myo4p, one of two class V myosins in budding yeast, continuously transports messenger RNA (mRNA) cargo in the cell but is nonprocessive when characterized in vitro. The adapter protein She3p tightly binds to the Myo4p rod, forming a single-headed motor complex. In this paper, we show that two Myo4p-She3p motors are recruited by the tetrameric mRNA-binding protein She2p to form a processive double-headed complex. The binding site for She3p was mapped to a single α helix that protrudes at right an ...[more]