Abstract

The development and implementation of the mass spectrometry core is essential to the research of the listed principal investigators. In particular the core will provide mass spectral analysis using the proposed bottomup and top-down methods employing both Q-TOF technology as well as FTICR high-resolution analysis. Both a top-down (intact protein identification) and a bottom-up (protein digestion) approach will be used to identify proteins of the various ribosomal complexes. Differences in post-translational modifications will be determined for ribosome complexes which have been subjected to infection by various viruses (hepatitis c, dengue, etc). eif3 factors associated with the ribosome will be analyzed and investigated for the presence of phosphorylation. Both the high-resolution capabilities of the exisiting FTICR and the sensitivity and flexibility of the Q-TOF, in combination with well established sample preparation methods such as IMAC, will allow for the unambiguous determination of protein constituents and associated post-translational modifications.

  Funding Agency

Agency
National Institute of Health (NIH)
Institute
National Institute of General Medical Sciences (NIGMS)
Type
Research Program Projects (P01)
Project #
5P01GM073732-05
Application #
8085778
Study Section
Special Emphasis Panel (ZRG1)
Project Start
Project End
Budget Start
2010-06-01
Budget End
2011-05-31
Support Year
5
Fiscal Year
2010
Total Cost
$147,717
Indirect Cost

  Institution

Name
University of California Berkeley
Department
Type
DUNS #
124726725
City
Berkeley
State
CA
Country
United States
Zip Code
94704

  Publications

Andaya, Armann; Villa, Nancy; Jia, Weitao et al. (2014) Phosphorylation stoichiometries of human eukaryotic initiation factors. Int J Mol Sci 15:11523-38
Kranzusch, Philip J; Lee, Amy Si-Ying; Berger, James M et al. (2013) Structure of human cGAS reveals a conserved family of second-messenger enzymes in innate immunity. Cell Rep 3:1362-8
Jia, Weitao; Andaya, Armann; Leary, Julie A (2012) Novel mass spectrometric method for phosphorylation quantification using cerium oxide nanoparticles and tandem mass tags. Anal Chem 84:2466-73
Sokabe, Masaaki; Fraser, Christopher S; Hershey, John W B (2012) The human translation initiation multi-factor complex promotes methionyl-tRNAi binding to the 40S ribosomal subunit. Nucleic Acids Res 40:905-13
Jäger, Stefanie; Cimermancic, Peter; Gulbahce, Natali et al. (2012) Global landscape of HIV-human protein complexes. Nature 481:365-70
Fuchs, Gabriele; Diges, Camille; Kohlstaedt, Lori A et al. (2011) Proteomic analysis of ribosomes: translational control of mRNA populations by glycogen synthase GYS1. J Mol Biol 410:118-30
Andaya, Armann; Jia, Weitao; Sokabe, Masaaki et al. (2011) Phosphorylation of human eukaryotic initiation factor 2?: novel site identification and targeted PKC involvement. J Proteome Res 10:4613-23
Sun, Chaomin; Todorovic, Aleksandar; Querol-Audí, Jordi et al. (2011) Functional reconstitution of human eukaryotic translation initiation factor 3 (eIF3). Proc Natl Acad Sci U S A 108:20473-8
Berry, Katherine E; Peng, Betty; Koditek, David et al. (2011) Optimized high-throughput screen for hepatitis C virus translation inhibitors. J Biomol Screen 16:211-20
Berry, Katherine E; Waghray, Shruti; Mortimer, Stefanie A et al. (2011) Crystal structure of the HCV IRES central domain reveals strategy for start-codon positioning. Structure 19:1456-66

Showing the most recent 10 out of 18 publications