Main Body
Investigators and Program Directors
Steven D. Hanes
Research Scientist, Wadsworth Center,
Molecular Genetics
Associate Professor, School of Public Health,
Biomedical Sciences
Ph.D., Brown University (1988)
Postdoctoral training, Massachusetts General Hospital/Harvard
Medical School
E-mail: hanes@wadsworth.org
Select Publications
- Singh, N., Ma, Z., Gemmill, T., Wu, X., Rossettini, A., Rabeler, C., Beane, O., DeFiglio, H., Palumbo, M., Morse, R. and Hanes, S. D. (2009). The Ess1 prolyl isomerase is required for transcription termination of small non-coding regulatory RNAs via the Nrd1 pathway. Mol. Cell, (in press Oct 23)
- Matyash, A., Singh, N., Hanes, S.D. and Jäckle, H. (2009). SAP18 promotes Krüppel-dependent transcriptional repression by enhancer-specific histone deacetylation. J. Biol. Chem. 284:3012-20.
- Horner, V. L., Czank, A., Jang, J. K., Singh, N., Williams, B. C., Puro, J., Kubli, E., Hanes, S. D., McKim, K. S., Wolfner, M. F. and Goldberg, M. (2006). The Drosophila calcipressin Sarah is required for several aspects of egg activation. Current Biol. 16: 1441-1446.
- Lebrecht, D., Foehr, M., Smith, E., Lopes, F.J. P., Vanario-Alonso C. E., Reinitz, J., Burz, D. S., and Hanes, S. D. (2005). Bicoid cooperative DNA binding is critical for embryonic patterning in Drosophila. Proc. Natl. Acad. Sci. USA 102:13176-13181
- Ren, P., Chaturvedi, V. and Hanes, S. D. (2005). The Ess1 prolyl isomerase is dispensable for growth but required for virulence in Cryptococcus neoformans. Microbiology 151: 1593-1605.
- Li, H-M, Li, Z., Devasahayam, G., Gemmill, T., Chaturvedi, V., Hanes, S. D., and Van Roey, P. (2005). Structure of the Candida albicans Ess1 prolyl isomerase reveals a well-ordered linker region that restricts domain mobility. Biochemistry 44: 6180-6189.
- Gemmill, T., Wu, X., and Hanes, S.D. (2005). Vanishingly low levels of Ess1 prolyl-isomerase activity are sufficient for growth in Saccharomyces cerevisiae. J. Biol. Chem. 280:15510-15517.
- Singh, N., Zhu, W. and Hanes, S. D. (2005). Sap18 is required for the maternal gene bicoid to direct anterior patterning in Drosophila melanogaster. Devel. Biol. 278: 242-254
- Wilcox, C. B., Rossettini, A. and Hanes, S. D. (2004). Genetic interactions with CTD kinases and the CTD of RNA pol II suggest a role for ESS1 in transcription initiation and elongation in Saccharomyces cerevisiae. Genetics 167:93-105.
- Habura, A., Pawlowski, J., Hanes., S. D., and Bowser, S. S. (2004). Unexpected foraminiferal diversity revealed by small-subunit rDNA analysis of Antarctic sediment. J Euk Microbiol 51, 173-179.
- Wu, X., Rossettini, A. and Hanes, S. D. (2003). The ESS1 prolyl isomerase and its suppressor BYE1 interact with RNA pol II to inhibit transcription elongation in Saccharomyces cerevisiae. Genetics 165:1687-1702.
- Devasahayam, G., Chaturvedi, V. and Hanes, S. D., (2002). The Ess1 prolyl-isomerase is essential for growth and morphogenetic switching in Candida albicans. Genetics 160: 37-48.
- Wu, X., Chang, A., Sudol, M. and Hanes, S. D. (2001). Genetic interactions between the ESS1 prolyl-isomerase and the RSP5 ubiquitin ligase reveal opposing effects on RNA polymerase II function. Current Genetics 40: 234-242.
- Burz, D. S. and Hanes, S. D. (2001). Isolation of mutations that disrupt cooperative DNA binding by the Drosophila Bicoid protein. J. Mol. Biol. 305: 219-230.
- Zhu, W., Foehr, M., Jaynes, J. B., and Hanes, S. D. (2001). Drosophila SAP18, a member of the Sin3/Rpd3 histone deacetylase complex interacts with Bicoid and inhibits its activity. Dev. Genes Evol. 211: 109 - 117.
- Wu, X., Wilcox, C. B., Devasahayam, G., Hackett, R.L., Arevalo-Rodriguez, M., Cardenas, M. and Hanes, S. D. (2000). The Ess1 prolyl-isomerase is linked to chromatin remodeling complexes and the general transcription machinery. EMBO J. 19:3727-3738.
- Zhu, W. and Hanes, S.D. (2000). Identification of Drosophila Bicoid-Interacting Proteins Using a Custom Two-Hybrid Selection. Gene 245:329-339.
- Burz, D.S., Rivera-Pomar, R., Jäckle, H., and Hanes, S.D. (1998). Cooperative DNA binding by Bicoid provides a mechanism for threshold-dependent activation in the Drosophila embryo. EMBO J. 17:5998-6009.
Contact Information
E-mail: hanes@wadsworth.org
