University of Iowa
Department of Biochemistry
4-403 BSB
Iowa City, IA 52242-1109 USA phone: 877-846-8569
or 319-335-7932
fax: (319) 335-9570
biochem@uiowa.edu

Department of Biochemistry

Professor of Biochemistry, PhD

Office: 4-452 BSB
Phone: (319) 335-7911
Fax: (319) 335-9570
peter-rubenstein@uiowa.edu

Peter A. Rubenstein
51 Newton Rd
Biochemistry/Univ. of Iowa
Iowa City, IA 52242

Research Interests

My research focuses on the factors that determine actin function in muscle and nonmuscle cells. We use site-directed mutagenesis coupled with a yeast expression system to make specific changes in yeast actin and to then assess the effects of these mutations in vivo and in vitro. Specific on-going projects involve a determination of the factors that allow formation of stable actin filaments, the role of the bound nucleotide in actin function, and the postulated role of tropomyosin as an actin-filament stabilizing protein.

Figure Legend. Tryptic peptide digest of wild-type and two mutant yeast actins with altered amino terminal regions. Mutations were made using site-directed mutagenesis. Arrows denote the peptides in which the mutations are located. A: wild-type actin; B: D2 and E4 altered to N and Q respectively; C: D2 - E4 deleted

Recent Publications

Shvetsov, A., Galkin, V.C., Orlova, A., Phillips, M., Bergeron, S.E., Rubenstein, P.A., Egelman, E.H., and Reisler, E. (2008) Actin hydrophobic loop 262-274 and filament nucleation and elongation. J. Mol. Biol. 375:793-801.

Wen, K.K., McKane, M., Houtman, J.C. and Rubenstein, P.A. (2008) Control of the ability of profilin to bind and facilitate nucleotide exchange from G-actin. J. Biol. Chem. 283-9444-9453.

Scoville, D., Stamm, J.D., Toledo-Warshaviak, D., Altenbach, C., Phillips, M., Shvetsov, A., Rubenstein, P.A., Hubbell, W.L., and Reisler, E. (2006) Hydrophobic loops dynamics and actin filament stability. Biochemistry 45:13576-13584.

McKane, M., Wen, K.K., Meyer, A., and Rubenstein, P.A. (2006) Effect of the substitute of muscle-actin-specific subdomain 1 and 2 residues in yeast actin on actin function. J. Biol. Chem. 281:29916-29928.

Bryan, K.E., Wen, K.-K., Zhu, M., Rendtorff, N.D., Feldkamp, M., Tranebjaerg, L., Friderici, K.H., and Rubenstein, P.A. (2006) Effects of human deafness g-actin mutations (DFNA20/26) on actin function. J. Biol. Chem. 281:20129-20139.

Chen, W., Wen, K.-K., Sens, A.E., and Rubenstein, P.A. (2006) Differential interactions of cardiac, skeletal muscle and yeast tropomyosins with fluorescent (Pyrene235) yeast actin. Biophys. J. 90:1308-1318.

Shvetsov, A., Stamm, J.D., Phillips, M., Warshaviak, D., Altenbach, C., Rubenstein, P.A., Hideg, K., Hubbell, W.L., and Reisler, E. (2006) Conformational dynamics of loop 262 - 274 in G- and F-actin. Biochemistry 45:6541-6549.

McKane, M., Wen, K.-K., Boldogh, I.R., Ramcharan, S., Pon, L.A., and Rubenstein, P.A. (2005) A mammalian actin substitution in yeast actin (H372R) causes a suppressible mitochondria/vacuole phenotype. J. Biol. Chem. 280:36494-36501.

Rubenstein, P.A. and Wen, K.K. (2005) Lights, camera, actin. IUBMB Life 57:683-687.

Wen, K.-K. and Rubenstein, P.A. (2005) Acceleration of yeast actin polymerization by yeast Arp2/3 complex does not require an Arp2/3-activating protein. J. Biol. Chem. 280:24168-24174.

Lu, X., Bryant, M.K., Bryan, K., Rubenstein, P.A., and Kawai, M. (2005) Role of the N-terminal negative charges of actin in force generation and cross-bridge kinetics in reconstituted bovine cardiac muscle fibres. J. Physiol. 564:65-82.

Bryan, K.E. and Rubenstein, P.A. (2005) An intermediate form of ADP-F actin. J. Biol. Chem 280:1696-1703.

Orlova, A., Shvetsov, A., Galkin, V.E., Kudryashov, D.S., Rubenstein, P.A., Egelman, E.H., and Reisler, E. (2004) Actin-destabilizing factors disrupt filaments by means of a time reversal of polymerization. Proc. Nat'l. Acad. Sci., USA 101:17664-17668.

Wen, K.-K., Blake, M.S., and Rubenstein, P.A. (2004) Neisseria Gonerrhoeae porin, P.IB, causes release of ATP from yeast G-actin. J. Mus. Res. & Cell Mot. 25:343-350.

Bartman, T., Walsh, E.C., Wen, K.-K., McKane, M., Ren, J., Alexander, J., Rubenstein, P.A. and Stainier, D.Y. (2004) Early Myocardial function affects endocardial cushion development in Zebrafish. PLoS Biology 2: 673-681.

Rubenstein, P.A. (2004) Alcohol Metabolism (A Song). Biochem & Molec Biol. Edu. 32: 30.

Wen, K.-K., and Rubenstein, P.A. (2003) Biochemical consequences of the Cardiofunk (R177H) mutation in yeast actin. J. Biol. Chem. 278: 48386-48394.

Vorobiev, S., Strokopytov, B., Drubin, D.G., Frieden, C., Ono, S., Condeelis, J., Rubenstein, P.A., and Almo, S.C. (2003) The structure of non-vertebrate actin: implications for the ATP hydrolytic mechanism. Proc. Nat. Acad. Sci., U.S.A., 100: 5760-5765.

Kusner, D.J., Barton, J.A., Wen, K.-K., Wang, X., Rubenstein, P.A., and Iyer, S.S. (2002) Regulation of phospholipase D activity by action. J. Biol. Chem. 277: 50683-50692.

Wong, W., Gerson, J., Rubenstein, P.A., and Reisler, E. (2002) Thin filament regulation and ionic contacts between the N-terminal region in actin and troponin. Biophys. J. 83: 2726-2732.

Shvetsov, A., Musib, R., Rubenstein, P.A., and Reisler, E. (2002) Locking the hydrophobic loop 262 - 274 to G-actin surface by a disulfide bridge prevents filament formation. Biochemistry, 41: 10787-10793.

Wen, K.-K., Yao, X., and Rubenstein, P.A. (2002) GTP-yeast actin. J. Biol. Chem. 277:: 41101-41109.

Yao, X., Nguyen, V., Wriggers, W., and Rubenstein, P.A. (2002) Regulation of yeast actin behavior by interaction of charged residues across the interdomain cleft. J. Biol. Chem. 277: 22875-22882.

Musib, R., Wang, G., Geng., L., and Rubenstein, P.A. (2002) Effect of polymerization on the subdomain 3/4 loop of yeast actin. J. Biol. Chem. 277:22699-22709.

Yao, X., and Rubenstein, P.A. (2001) F-Actin like ATPase activity in a polymerization-defective mutant yeast sctin (V266G/L267G). J. Biol. Chem. 276: 25598-25604.

Affiliations

Biochemistry Department
Molecular and Cellular Biology Program