SUS1/YBR111W-A Literature Guide Help

Other names published for SUS1: YBR111W-A

SUS1 - Protein-protein Interactions (21)

ReferenceOther Genes Addressed
Diebold ML, et al.  (2011) Deciphering correct strategies for multiprotein complex assembly by co-expression: application to complexes as large as the histone octamer. J Struct Biol 175(2):178-88
Lee KK, et al.  (2011) Combinatorial depletion analysis to assemble the network architecture of the SAGA and ADA chromatin remodeling complexes. Mol Syst Biol 7():503
Bonnet J, et al.  (2010) The structural plasticity of SCA7 domains defines their differential nucleosome-binding properties. EMBO Rep 11(8):612-8
Cuenca-Bono B, et al.  (2010) A novel link between Sus1 and the cytoplasmic mRNA decay machinery suggests a broad role in mRNA metabolism. BMC Cell Biol 11():19
Ellisdon AM, et al.  (2010) Structural basis for the interaction between yeast Spt-Ada-Gcn5 acetyltransferase (SAGA) complex components Sgf11 and Sus1. J Biol Chem 285(6):3850-6
Kohler A, et al.  (2010) Structural basis for assembly and activation of the heterotetrameric SAGA histone H2B deubiquitinase module. Cell 141(4):606-17
Samara NL, et al.  (2010) Structural insights into the assembly and function of the SAGA deubiquitinating module. Science 328(5981):1025-9
Hossain MA, et al.  (2009) The cap binding complex influences H2B ubiquitination by facilitating splicing of the SUS1 pre-mRNA. RNA 15(8):1515-27
Jani D, et al.  (2009) Sus1, Cdc31, and the Sac3 CID region form a conserved interaction platform that promotes nuclear pore association and mRNA export. Mol Cell 33(6):727-37
Klockner C, et al.  (2009) Mutational Uncoupling of the Role of Sus1 in Nuclear Pore Complex Targeting of an mRNA Export Complex and Histone H2B Deubiquitination. J Biol Chem 284(18):12049-56
Lee KK, et al.  (2009) Yeast Sgf73/Ataxin-7 serves to anchor the deubiquitination module into both SAGA and Slik(SALSA) HAT complexes. Epigenetics Chromatin 2(1):2
Mischerikow N, et al.  (2009) In-depth profiling of post-translational modifications on the related transcription factor complexes TFIID and SAGA. J Proteome Res 8(11):5020-30
Chekanova JA, et al.  (2008) Sus1, Sac3, and Thp1 mediate post-transcriptional tethering of active genes to the nuclear rim as well as to non-nascent mRNP. RNA 14(1):66-77
Kohler A, et al.  (2008) Yeast Ataxin-7 links histone deubiquitination with gene gating and mRNA export. Nat Cell Biol 10(6):707-15
Pascual-Garcia P, et al.  (2008) Sus1 is recruited to coding regions and functions during transcription elongation in association with SAGA and TREX2. Genes Dev 22(20):2811-22
Oeffinger M, et al.  (2007) Comprehensive analysis of diverse ribonucleoprotein complexes. Nat Methods 4(11):951-6
Kohler A, et al.  (2006) The mRNA export factor Sus1 is involved in Spt/Ada/Gcn5 acetyltransferase-mediated H2B deubiquitinylation through its interaction with Ubp8 and Sgf11. Mol Biol Cell 17(10):4228-36
Lee D, et al.  (2005) The proteasome regulatory particle alters the SAGA coactivator to enhance its interactions with transcriptional activators. Cell 123(3):423-36
Fischer T, et al.  (2004) Yeast centrin Cdc31 is linked to the nuclear mRNA export machinery. Nat Cell Biol 6(9):840-8
Rodriguez-Navarro S, et al.  (2004) Sus1, a functional component of the SAGA histone acetylase complex and the nuclear pore-associated mRNA export machinery. Cell 116(1):75-86
Wu PY, et al.  (2004) Molecular architecture of the S. cerevisiae SAGA complex. Mol Cell 15(2):199-208