[Arabidopsis] Post-doc position in RNA biology

Dr. Sarah Assmann sma3 at psu.edu
Tue Mar 21 11:38:45 EST 2006


POST-DOCTORAL POSITION IN RNA BIOLOGY
Penn State University, University Park, PA, USA

      A post-doctoral position is available to study dynamic regulation of 
RNA processing by a small family of Arabidopsis hnRNP-type RNA binding 
proteins. This project is a collaboration between a plant biology group, 
headed by Prof. Sally Assmann: 
(<http://www.bio.psu.edu/People/Faculty/Assmann/lab/>http://www.bio.psu.edu/People/Faculty/Assmann/lab/ 
), and an
RNA chemistry group, headed by Prof. Phil Bevilacqua: 
(<http://research.chem.psu.edu/pcbgroup/>http://research.chem.psu.edu/pcbgroup/). 
The successful applicant will have the opportunity to expand his or her 
knowledge of biochemical and structural approaches to understanding RNA 
biology, and to investigate the roles of these RNA binding proteins in 
overall plant growth and development.
      Applicants should have a Ph.D. in the one of biosciences or in a 
closely related area, should have published in international journals, and 
should have excellent communication skills. Applicants should have 
demonstrated expertise in RNA biology and/or protein biochemistry and in 
Arabidopsis molecular genetics. Interested applicants should send via 
e-mail a cover letter, a c.v., and pdfs of published or in press articles 
to <mailto:abpostdoc at psu.edu>abpostdoc at bio.psu.edu. Applicants currently 
residing in North America or Europe should also arrange to have two letters 
of reference sent to the same e-mail address.

Related Publications

Li, J., Kinoshita, K., Pandey, S., Ng, C K-Y., Gygi, S.P., Shimazaki, K-I., 
and Assmann, S.M. 2002. Modulation of an RNA-binding protein by 
abscisic-acid-activated kinase. Nature 418: 793-797.

Zheng, X. and Bevilacqua, P. C. 2004. Activation of the protein kinase PKR 
by short double-stranded RNAs with single-stranded tails. RNA 10: 1934-1945.

Nakano, S., Chadalavada, D. M. and Bevilacqua, P. C. 2000. General 
acid-base catalysis in the mechanism of a hepatitis delta virus ribozyme. 
Science 287: 1493-1497.

AA/EOE


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