Journal article
Functional Adaptation between Yeast Actin and Its Cognate Myosin Motors
The Journal of biological chemistry, Vol.286(35), pp.30384-30392
09/02/2011
DOI: 10.1074/jbc.M111.262899
PMCID: PMC3162397
PMID: 21757693
Abstract
We employed budding yeast and skeletal muscle actin to examine the contribution of the actin isoform to myosin motor function. While yeast and muscle actin are highly homologous, they exhibit different charge density at their N termini (a proposed myosin-binding interface). Muscle myosin-II actin-activated ATPase activity is significantly higher with muscle
versus
yeast actin. Whether this reflects inefficiency in the ability of yeast actin to activate myosin is not known. Here we optimized the isolation of two yeast myosins to assess actin function in a homogenous system. Yeast myosin-II (Myo1p) and myosin-V (Myo2p) accommodate the reduced N-terminal charge density of yeast actin, showing greater activity with yeast over muscle actin. Increasing the number of negative charges at the N terminus of yeast actin from two to four (as in muscle) had little effect on yeast myosin activity, while other substitutions of charged residues at the myosin interface of yeast actin reduced activity. Thus, yeast actin functions most effectively with its native myosins, which in part relies on associations mediated by its outer domain. Compared with yeast myosin-II and myosin-V, muscle myosin-II activity was very sensitive to salt. Collectively, our findings suggest differing degrees of reliance on electrostatic interactions during weak actomyosin binding in yeast
versus
muscle. Our study also highlights the importance of native actin isoforms when considering the function of myosins.
Details
- Title: Subtitle
- Functional Adaptation between Yeast Actin and Its Cognate Myosin Motors
- Creators
- Benjamin C Stark - From theKuo-Kuang Wen - theJohn S Allingham - thePeter A Rubenstein - theMatthew Lord - From the
- Resource Type
- Journal article
- Publication Details
- The Journal of biological chemistry, Vol.286(35), pp.30384-30392
- DOI
- 10.1074/jbc.M111.262899
- PMID
- 21757693
- PMCID
- PMC3162397
- NLM abbreviation
- J Biol Chem
- ISSN
- 0021-9258
- eISSN
- 1083-351X
- Publisher
- American Society for Biochemistry and Molecular Biology; 9650 Rockville Pike, Bethesda, MD 20814, U.S.A
- Grant note
- GM33689 / National Institutes of Health
- Alternative title
- Influence of the Actin Isoform on Yeast Myosins
- Language
- English
- Date published
- 09/02/2011
- Academic Unit
- Stead Family Department of Pediatrics; Biochemistry and Molecular Biology; Internal Medicine
- Record Identifier
- 9984024564902771
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