HTA2

Summary

Gene Symbol: HTA2
Description: histone H2A
Alias: H2A2, histone H2A
Species: Saccharomyces cerevisiae S288c
Products:     HTA2

Top Publications

  1. Yang X, Zaurin R, Beato M, Peterson C. Swi3p controls SWI/SNF assembly and ATP-dependent H2A-H2B displacement. Nat Struct Mol Biol. 2007;14:540-7 pubmed
    ..Our data indicate that H2A-H2B dimer loss is not an obligatory consequence of ATP-dependent DNA translocation, and furthermore they suggest that SWI/SNF is composed of at least four interdependent modules. ..
  2. VanDemark A, Blanksma M, Ferris E, Heroux A, Hill C, Formosa T. The structure of the yFACT Pob3-M domain, its interaction with the DNA replication factor RPA, and a potential role in nucleosome deposition. Mol Cell. 2006;22:363-74 pubmed
    ..These results support the model that the FACT family has an essential role in constructing nucleosomes during DNA replication, and suggest that RPA contributes to this process. ..
  3. Javaheri A, Wysocki R, Jobin Robitaille O, Altaf M, Cote J, Kron S. Yeast G1 DNA damage checkpoint regulation by H2A phosphorylation is independent of chromatin remodeling. Proc Natl Acad Sci U S A. 2006;103:13771-6 pubmed
    ..b>Histone H2A (yeast H2AX) is rapidly phosphorylated on S129 by the kinase Tel1 (ATM) over a domain extending kilobases from ..
  4. Clarke A, Lowell J, Jacobson S, Pillus L. Esa1p is an essential histone acetyltransferase required for cell cycle progression. Mol Cell Biol. 1999;19:2515-26 pubmed
    ..These observations therefore link an essential HAT activity to cell cycle progression, potentially through discrete transcriptional regulatory events. ..
  5. Wu W, Alami S, Luk E, Wu C, Sen S, Mizuguchi G, et al. Swc2 is a widely conserved H2AZ-binding module essential for ATP-dependent histone exchange. Nat Struct Mol Biol. 2005;12:1064-71 pubmed
    ..H2AZ is mediated by the multiprotein SWR1 complex, which catalyzes ATP-dependent exchange of nucleosomal histone H2A for H2AZ...
  6. Park Y, Sudhoff K, Andrews A, Stargell L, Luger K. Histone chaperone specificity in Rtt109 activation. Nat Struct Mol Biol. 2008;15:957-64 pubmed
    ..Nap1 and Vps75 interact with histones and Rtt109 with comparable affinities. However, only Vps75 stimulates Rtt109 enzymatic activity. Our data highlight the functional specificity of Vps75 in Rtt109 activation. ..
  7. Camahort R, Shivaraju M, Mattingly M, Li B, Nakanishi S, Zhu D, et al. Cse4 is part of an octameric nucleosome in budding yeast. Mol Cell. 2009;35:794-805 pubmed publisher
    ..Taken together, our experimental evidence supports the model that the Cse4 nucleosome is an octamer, containing two copies each of Cse4, H2A, H2B, and H4. ..
  8. Morillo Huesca M, Maya D, Muñoz Centeno M, Singh R, Oreal V, Reddy G, et al. FACT prevents the accumulation of free histones evicted from transcribed chromatin and a subsequent cell cycle delay in G1. PLoS Genet. 2010;6:e1000964 pubmed publisher
  9. Tomson B, Davis C, Warner M, Arndt K. Identification of a role for histone H2B ubiquitylation in noncoding RNA 3'-end formation through mutational analysis of Rtf1 in Saccharomyces cerevisiae. Genetics. 2011;188:273-89 pubmed publisher

More Information

Publications47

  1. Lindstrom K, Vary J, Parthun M, Delrow J, Tsukiyama T. Isw1 functions in parallel with the NuA4 and Swr1 complexes in stress-induced gene repression. Mol Cell Biol. 2006;26:6117-29 pubmed
    ..In contrast to a recruitment-based model, we find that the NuA4 and Swr1 complexes act throughout the genome while only a specific subset of the genome shows alterations in transcription. ..
  2. Mitsumori R, Shinmyozu K, Nakayama J, Uchida H, Oki M. Gic1 is a novel heterochromatin boundary protein in vivo. Genes Genet Syst. 2016;91:151-159 pubmed
    ..Moreover, we performed domain analysis to identify domain(s) of Gic1 that are important for its boundary activity, and identified two minimum domains, which are located outside its Cdc42-binding domain. ..
  3. Calvert M, Keck K, Ptak C, Shabanowitz J, Hunt D, Pemberton L. Phosphorylation by casein kinase 2 regulates Nap1 localization and function. Mol Cell Biol. 2008;28:1313-25 pubmed
    ..In conclusion, our data show that Nap1 phosphorylation by CK2 appears to regulate Nap1 localization and is required for normal progression through S phase. ..
  4. Tian R, Hoa X, Lambert J, Pezacki J, Veres T, Figeys D. Development of a multiplexed microfluidic proteomic reactor and its application for studying protein-protein interactions. Anal Chem. 2011;83:4095-102 pubmed publisher
  5. Meas R, Smerdon M, Wyrick J. The amino-terminal tails of histones H2A and H3 coordinate efficient base excision repair, DNA damage signaling and postreplication repair in Saccharomyces cerevisiae. Nucleic Acids Res. 2015;43:4990-5001 pubmed publisher
    ..In summary, our data identify novel roles of the histone H2A and H3 N-tails in (i) regulating the expression of a critical BER enzyme (Mag1), (ii) supporting efficient DNA ..
  6. Fukuma M, Hiraoka Y, Sakurai H, Fukasawa T. Purification of yeast histones competent for nucleosome assembly in vitro. Yeast. 1994;10:319-31 pubmed
    ..The length of DNA fragment wrapping around a core histone particle and the molar ratio of histone components in an assembled nucleosome particle were estimated to be 150 +/- 10 bp long and H2A:H2B:H3:H4 = 1.0:0.9:0:9:1.0, respectively. ..
  7. Eapen V, Sugawara N, Tsabar M, Wu W, Haber J. The Saccharomyces cerevisiae chromatin remodeler Fun30 regulates DNA end resection and checkpoint deactivation. Mol Cell Biol. 2012;32:4727-40 pubmed publisher
    ..2 kb/h. We also found that the resection rate is reduced by DNA damage-induced phosphorylation of histone H2A-S129 (?-H2AX) and that Fun30 interacts preferentially with nucleosomes in which H2A-S129 is not phosphorylated...
  8. Zheng S, Crickard J, Srikanth A, Reese J. A highly conserved region within H2B is important for FACT to act on nucleosomes. Mol Cell Biol. 2014;34:303-14 pubmed publisher
    ..We have uncovered a previously unappreciated role for the HBR domain in regulating chromatin structure and have provided insight into how FACT acts on nucleosomes. ..
  9. Syntichaki P, Thireos G. The Gcn5.Ada complex potentiates the histone acetyltransferase activity of Gcn5. J Biol Chem. 1998;273:24414-9 pubmed
    ..Because Ada2 is required for the assembly of Gcn5, we conclude that one role for components of the Gcn5.Ada complex is the potentiation of its HAT activity. ..
  10. Onishi M, Liou G, Buchberger J, Walz T, Moazed D. Role of the conserved Sir3-BAH domain in nucleosome binding and silent chromatin assembly. Mol Cell. 2007;28:1015-28 pubmed
    ..Together, these observations suggest that the SIR complex associates with an extended chromatin fiber through interactions with two different regions in the nucleosome. ..
  11. Grunstein M. Histone function in transcription. Annu Rev Cell Biol. 1990;6:643-78 pubmed
  12. Morillo Huesca M, Clemente Ruiz M, Andújar E, Prado F. The SWR1 histone replacement complex causes genetic instability and genome-wide transcription misregulation in the absence of H2A.Z. PLoS ONE. 2010;5:e12143 pubmed publisher
    The SWR1 complex replaces the canonical histone H2A with the variant H2A.Z (Htz1 in yeast) at specific chromatin regions...
  13. Bazzi M, Mantiero D, Trovesi C, Lucchini G, Longhese M. Dephosphorylation of gamma H2A by Glc7/protein phosphatase 1 promotes recovery from inhibition of DNA replication. Mol Cell Biol. 2010;30:131-45 pubmed publisher
    ..Furthermore, Glc7 counteracts in vivo histone H2A phosphorylation on serine 129 (gamma H2A) and dephosphorylates gamma H2A in vitro...
  14. Redon C, Pilch D, Bonner W. Genetic analysis of Saccharomyces cerevisiae H2A serine 129 mutant suggests a functional relationship between H2A and the sister-chromatid cohesion partners Csm3-Tof1 for the repair of topoisomerase I-induced DNA damage. Genetics. 2006;172:67-76 pubmed
    ..Our genetic studies suggest a role for H2A serine 129 in the establishment of specialized cohesion structure necessary for the normal repair of topoisomerase I-induced DNA damage. ..
  15. Hammet A, Magill C, Heierhorst J, Jackson S. Rad9 BRCT domain interaction with phosphorylated H2AX regulates the G1 checkpoint in budding yeast. EMBO Rep. 2007;8:851-7 pubmed
    Phosphorylation of histone H2A or H2AX is an early and sensitive marker of DNA damage in eukaryotic cells, although mutation of the conserved damage-dependent phosphorylation site is well tolerated...
  16. Masumoto H, Hawke D, Kobayashi R, Verreault A. A role for cell-cycle-regulated histone H3 lysine 56 acetylation in the DNA damage response. Nature. 2005;436:294-8 pubmed
    ..We suggest that the acetylation of histone H3 K56 creates a favourable chromatin environment for DNA repair and that a key component of the DNA damage response is to preserve this acetylation. ..
  17. Wu F, Liu Y, Zhu Z, Huang H, Ding B, Wu J, et al. The 1.9Å crystal structure of Prp20p from Saccharomyces cerevisiae and its binding properties to Gsp1p and histones. J Struct Biol. 2011;174:213-22 pubmed publisher
    ..Our model reveals that Prp20p and RCC1 share similar Ran GTPase binding mode. In addition, we also studied the histone-binding property of Prp20p in vitro. ..
  18. Rothenbusch U, Sawatzki M, Chang Y, Caesar S, Schlenstedt G. Sumoylation regulates Kap114-mediated nuclear transport. EMBO J. 2012;31:2461-72 pubmed publisher
    ..Remarkably, sumoylation of Kap114 greatly stimulates cargo dissociation in vitro. We propose that sumoylation occurs at the site of Kap114 cargo function and that SUMO is a cargo release factor involved in intranuclear targeting. ..
  19. Xu F, Zhang K, Grunstein M. Acetylation in histone H3 globular domain regulates gene expression in yeast. Cell. 2005;121:375-85 pubmed
    ..These findings indicate that histone H3 K56 acetylation at the entry-exit gate enables recruitment of the SWI/SNF nucleosome remodeling complex and so regulates gene activity. ..
  20. Ohouo P, Bastos de Oliveira F, Liu Y, Ma C, Smolka M. DNA-repair scaffolds dampen checkpoint signalling by counteracting the adaptor Rad9. Nature. 2013;493:120-4 pubmed publisher
    ..complex counteracts the checkpoint adaptor Rad9 by physically interacting with Dpb11 and phosphorylated histone H2A, two positive regulators of Rad9-dependent Rad53 activation...
  21. Westermann S, Cheeseman I, Anderson S, Yates J, Drubin D, Barnes G. Architecture of the budding yeast kinetochore reveals a conserved molecular core. J Cell Biol. 2003;163:215-22 pubmed
    ..We propose that a molecular core consisting of CENP-A, -C, -H, and Ndc80/HEC has been conserved from yeast to humans to link centromeres to spindle microtubules. ..
  22. Harvey A, Jackson S, Downs J. Saccharomyces cerevisiae histone H2A Ser122 facilitates DNA repair. Genetics. 2005;170:543-53 pubmed
    ..We previously demonstrated that Ser129 in the carboxyl-terminal tail of yeast histone H2A is important for double-strand-break responses...
  23. Grant P, Eberharter A, John S, Cook R, Turner B, Workman J. Expanded lysine acetylation specificity of Gcn5 in native complexes. J Biol Chem. 1999;274:5895-900 pubmed
    ..Furthermore Ada and SAGA have overlapping, yet distinct, patterns of acetylation, suggesting that the association of specific subunits determines site specificity. ..
  24. Hodges J, Leslie J, Mosammaparast N, Guo Y, Shabanowitz J, Hunt D, et al. Nuclear import of TFIIB is mediated by Kap114p, a karyopherin with multiple cargo-binding domains. Mol Biol Cell. 2005;16:3200-10 pubmed
    ..The import of more than one cargo at a time would increase the efficiency of each import cycle and may allow the regulation of coimported cargoes. ..
  25. Liu H, Zhang M, He W, Zhu Z, Teng M, Gao Y, et al. Structural insights into yeast histone chaperone Hif1: a scaffold protein recruiting protein complexes to core histones. Biochem J. 2014;462:465-73 pubmed publisher
    ..By binding to the core histone complex Hif1 may recruit functional protein complexes to modify histones during chromatin reassembly. ..
  26. Dechassa M, Wyns K, Luger K. Scm3 deposits a (Cse4-H4)2 tetramer onto DNA through a Cse4-H4 dimer intermediate. Nucleic Acids Res. 2014;42:5532-42 pubmed publisher
    ..Moreover, we demonstrate that Cse4 and H3 are structurally compatible to be incorporated in the same nucleosome to form heterotypic particles. Our data shed light on the mechanism of Scm3-mediated nucleosome assembly at the centromere. ..
  27. Vázquez Martin C, Rouse J, Cohen P. Characterization of the role of a trimeric protein phosphatase complex in recovery from cisplatin-induced versus noncrosslinking DNA damage. FEBS J. 2008;275:4211-21 pubmed publisher
  28. Najor N, Weatherford L, Brush G. Prevention of DNA Rereplication Through a Meiotic Recombination Checkpoint Response. G3 (Bethesda). 2016;6:3869-3881 pubmed publisher
    ..Phosphorylation of histone H2A, which is catalyzed by Mec1 and the related Tel1 protein kinase in response to DSBs, and can help coordinate ..
  29. Wyce A, Xiao T, Whelan K, Kosman C, Walter W, Eick D, et al. H2B ubiquitylation acts as a barrier to Ctk1 nucleosomal recruitment prior to removal by Ubp8 within a SAGA-related complex. Mol Cell. 2007;27:275-88 pubmed
    ..These findings reveal a mechanism by which H2B ubiquitylation acts as a barrier to Ctk1 association with active genes, while subsequent deubiquitylation by Ubp8 triggers Ctk1 recruitment at the appropriate point in activation. ..
  30. Valieva M, Armeev G, Kudryashova K, Gerasimova N, Shaytan A, Kulaeva O, et al. Large-scale ATP-independent nucleosome unfolding by a histone chaperone. Nat Struct Mol Biol. 2016;23:1111-1116 pubmed publisher
    ..Thus, FACT-dependent nucleosome unfolding modulates the accessibility of nucleosomal DNA, and this activity is an important function of FACT in vivo. ..
  31. Keogh M, Kim J, Downey M, Fillingham J, Chowdhury D, Harrison J, et al. A phosphatase complex that dephosphorylates gammaH2AX regulates DNA damage checkpoint recovery. Nature. 2006;439:497-501 pubmed
    ..Budding-yeast histone H2A is phosphorylated in a similar manner by the checkpoint kinases Tel1 and Mec1 (ref...
  32. Luk E, Vu N, Patteson K, Mizuguchi G, Wu W, Ranjan A, et al. Chz1, a nuclear chaperone for histone H2AZ. Mol Cell. 2007;25:357-68 pubmed
    ..of H2AZ into chromatin is dependent on the SWR1 complex, which catalyses the replacement of conventional histone H2A with H2AZ...
  33. Mosammaparast N, Del Rosario B, Pemberton L. Modulation of histone deposition by the karyopherin kap114. Mol Cell Biol. 2005;25:1764-78 pubmed
    ..Our results indicate a novel mechanism by which cells can regulate histone deposition and establish a coordinate link between histone nuclear import and chromatin assembly. ..
  34. Chittuluru J, Chaban Y, Monnet Saksouk J, Carrozza M, Sapountzi V, Selleck W, et al. Structure and nucleosome interaction of the yeast NuA4 and Piccolo-NuA4 histone acetyltransferase complexes. Nat Struct Mol Biol. 2011;18:1196-203 pubmed publisher
    ..homolog of mammalian Ing1 2 (Yng2) apparently positions Piccolo for efficient acetylation of histone H4 or histone H2A tails...
  35. Gilbert T, McDaniel S, Byrum S, Cades J, Dancy B, Wade H, et al. A PWWP domain-containing protein targets the NuA3 acetyltransferase complex via histone H3 lysine 36 trimethylation to coordinate transcriptional elongation at coding regions. Mol Cell Proteomics. 2014;13:2883-95 pubmed publisher
    ..Collectively, these studies define a new form of the NuA3 complex that associates with H3K36me3 to effect transcriptional elongation. MS data are available via ProteomeXchange with identifier PXD001156. ..
  36. Tessarz P, Santos Rosa H, Robson S, Sylvestersen K, Nelson C, Nielsen M, et al. Glutamine methylation in histone H2A is an RNA-polymerase-I-dedicated modification. Nature. 2014;505:564-8 pubmed publisher
    ..Here we describe a new class of histone modification, methylation of glutamine, occurring on yeast histone H2A at position 105 (Q105) and human H2A at Q104...
  37. Ranjan A, Wang F, Mizuguchi G, Wei D, Huang Y, Wu C. H2A histone-fold and DNA elements in nucleosome activate SWR1-mediated H2A.Z replacement in budding yeast. elife. 2015;4:e06845 pubmed publisher
    ..Z by a multi-step histone replacement reaction, evicting histone H2A-H2B from the canonical nucleosome and depositing the H2A.Z-H2B dimer...
  38. Park Y, Luger K. The structure of nucleosome assembly protein 1. Proc Natl Acad Sci U S A. 2006;103:1248-53 pubmed
    ..To our knowledge, this is the first structure of a member of the large NAP family of proteins and suggests a mechanism by which the shuttling of histones to and from the nucleus is regulated. ..