PT  - JOURNAL ARTICLE
AU  - Aaron D. Rosenbloom
AU  - Thomas D. Pollard
TI  - Interaction of the Proline-Rich Domain of Fission Yeast WASp (Ws1p1) with Actin Filaments
AID  - 10.1101/2022.01.26.477833
DP  - 2022 Jan 01
TA  - bioRxiv
PG  - 2022.01.26.477833
4099  - http://biorxiv.org/content/early/2022/01/26/2022.01.26.477833.short
4100  - http://biorxiv.org/content/early/2022/01/26/2022.01.26.477833.full
AB  - Background The Wiskott-Aldrich Syndrome protein (WASp) family of proteins plays a crucial role in the activation of the Arp2/3 (actin-related protein 2/3) complex to promote the branching of actin filaments. The proline-rich domain (PRD) of WASp is known to contribute to branching nucleation but was overlooked, until experiments showed that the PRD of budding yeast Las17 can bind actin filaments (1).Methods We purified recombinant proline-rich domains from fission yeast S. pombe Wsp1 and budding yeast S. cerevisiae Las17 to test in biochemical assays of actin binding and polymerization.Results The PRD of the S. pombe Wsp1 binds actin filaments with micromolar affinity. The PRDs of both Wsp1 and Las17 slowed the rate of actin filament elongation by Mg-ATP-actin monomers by half and slowed the spontaneous polymerization of Mg-ATP-actin monomers modestly.Conclusion The affinity of PRDs of WASp-family proteins for actin filaments is high enough to contribute to the reported stimulation of actin filament branching by Arp2/3 complex.Competing Interest StatementThe authors have declared no competing interest.