HTZ1/YOL012C Literature Guide Help

Other names published for HTZ1: HTA3, H2A.F/Z, H2AZ, YOL012C

HTZ1 - Protein-protein Interactions (27)

ReferenceOther Genes Addressed
Chen J, et al.  (2012) Single-molecule tools elucidate H2A.Z nucleosome composition. J Cell Sci 125(Pt 12):2954-64
Haas J, et al.  (2012) Physical links between the nuclear envelope protein Mps3, three alternate replication factor C complexes, and a variant histone in Saccharomyces cerevisiae. DNA Cell Biol 31(6):917-24
Armache KJ, et al.  (2011) Structural basis of silencing: Sir3 BAH domain in complex with a nucleosome at 3.0 A resolution. Science 334(6058):977-82
Gardner JM, et al.  (2011) Targeting of the SUN protein Mps3 to the inner nuclear membrane by the histone variant H2A.Z. J Cell Biol 193(3):489-507
Mahapatra S, et al.  (2011) Yeast H2A.Z, FACT complex and RSC regulate transcription of tRNA gene through differential dynamics of flanking nucleosomes. Nucleic Acids Res 39(10):4023-34
Tian R, et al.  (2011) Development of a multiplexed microfluidic proteomic reactor and its application for studying protein-protein interactions. Anal Chem 83(11):4095-102
Wang AY, et al.  (2011) Key functional regions in the histone variant H2A.Z C-terminal docking domain. Mol Cell Biol 31(18):3871-84
Luk E, et al.  (2010) Stepwise Histone Replacement by SWR1 Requires Dual Activation with Histone H2A.Z and Canonical Nucleosome. Cell 143(5):725-36
Straube K, et al.  (2010) Nap1 and Chz1 have separate Htz1 nuclear import and assembly functions. Traffic 11(2):185-97
Dai Z, et al.  (2009) Genome-wide analysis of interactions between ATP-dependent chromatin remodeling and histone modifications. BMC Genomics 10:304
Hansen DF, et al.  (2009) Binding kinetics of histone chaperone Chz1 and variant histone H2A.Z-H2B by relaxation dispersion NMR spectroscopy. J Mol Biol 387(1):1-9
Johnson A, et al.  (2009) Reconstitution of heterochromatin-dependent transcriptional gene silencing. Mol Cell 35(6):769-81
Koerber RT, et al.  (2009) Interaction of transcriptional regulators with specific nucleosomes across the Saccharomyces genome. Mol Cell 35(6):889-902
Martino F, et al.  (2009) Reconstitution of yeast silent chromatin: multiple contact sites and O-AADPR binding load SIR complexes onto nucleosomes in vitro. Mol Cell 33(3):323-34
Wu WH, et al.  (2009) N Terminus of Swr1 Binds to Histone H2AZ and Provides a Platform for Subunit Assembly in the Chromatin Remodeling Complex. J Biol Chem 284(10):6200-7
Pitre S, et al.  (2008) Global investigation of protein-protein interactions in yeast Saccharomyces cerevisiae using re-occurring short polypeptide sequences. Nucleic Acids Res 36(13):4286-94
Schluter C, et al.  (2008) Global Analysis of Yeast Endosomal Transport Identifies the Vps55/68 Sorting Complex. Mol Biol Cell 19(4):1282-1294
Larsen P, et al.  (2007) A statistical method to incorporate biological knowledge for generating testable novel gene regulatory interactions from microarray experiments. BMC Bioinformatics 8:317
Luk E, et al.  (2007) Chz1, a Nuclear Chaperone for Histone H2AZ. Mol Cell 25(3):357-68
Ramaswamy A and Ioshikhes I  (2007) Global dynamics of newly constructed oligonucleosomes of conventional and variant H2A.Z histone. BMC Struct Biol 7():76
Lebaron S, et al.  (2005) The splicing ATPase prp43p is a component of multiple preribosomal particles. Mol Cell Biol 25(21):9269-82
Wu WH, et al.  (2005) Swc2 is a widely conserved H2AZ-binding module essential for ATP-dependent histone exchange. Nat Struct Mol Biol 12(12):1064-71
Downs JA, et al.  (2004) Binding of chromatin-modifying activities to phosphorylated histone H2A at DNA damage sites. Mol Cell 16(6):979-90
Kobor MS, et al.  (2004) A protein complex containing the conserved Swi2/Snf2-related ATPase Swr1p deposits histone variant H2A.Z into euchromatin. PLoS Biol 2(5):E131
Mizuguchi G, et al.  (2004) ATP-driven exchange of histone H2AZ variant catalyzed by SWR1 chromatin remodeling complex. Science 303(5656):343-8
Adam M, et al.  (2001) H2A.Z is required for global chromatin integrity and for recruitment of RNA polymerase II under specific conditions. Mol Cell Biol 21(18):6270-9
Dhillon N and Kamakaka RT  (2000) A histone variant, Htz1p, and a Sir1p-like protein, Esc2p, mediate silencing at HMR. Mol Cell 6(4):769-80