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  1. Article: Structure of the yeast histone acetyltransferase Hat1: insights into substrate specificity and implications for the Gcn5-related N-acetyltransferase superfamily.

    Dutnall, R N / Tafrov, S T / Sternglanz, R / Ramakrishnan, V

    Cold Spring Harbor symposia on quantitative biology

    1998  Volume 63, Page(s) 501–507

    MeSH term(s) Acetyltransferases/chemistry ; Acetyltransferases/genetics ; Acetyltransferases/metabolism ; Amino Acid Sequence ; Animals ; Binding Sites ; Catalysis ; Histone Acetyltransferases ; Histones/chemistry ; Histones/metabolism ; Humans ; Molecular Sequence Data ; Protein Structure, Secondary ; Saccharomyces cerevisiae/enzymology ; Saccharomyces cerevisiae Proteins ; Substrate Specificity
    Chemical Substances Histones ; Saccharomyces cerevisiae Proteins ; Acetyltransferases (EC 2.3.1.-) ; Histone Acetyltransferases (EC 2.3.1.48) ; histone acetyltransferase type B complex (EC 2.3.1.48)
    Language English
    Publishing date 1998
    Publishing country United States
    Document type Journal Article ; Review
    ISSN 0091-7451
    ISSN 0091-7451
    DOI 10.1101/sqb.1998.63.501
    Database MEDical Literature Analysis and Retrieval System OnLINE

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  2. Article: Structure of the histone acetyltransferase Hat1: a paradigm for the GCN5-related N-acetyltransferase superfamily.

    Dutnall, R N / Tafrov, S T / Sternglanz, R / Ramakrishnan, V

    Cell

    1998  Volume 94, Issue 4, Page(s) 427–438

    Abstract: We have solved the crystal structure of the yeast histone acetyltransferase Hat1-acetyl coenzyme A (AcCoA) complex at 2.3 A resolution. Hat1 has an elongated, curved structure, and the AcCoA molecule is bound in a cleft on the concave surface of the ... ...

    Abstract We have solved the crystal structure of the yeast histone acetyltransferase Hat1-acetyl coenzyme A (AcCoA) complex at 2.3 A resolution. Hat1 has an elongated, curved structure, and the AcCoA molecule is bound in a cleft on the concave surface of the protein, marking the active site of the enzyme. A channel of variable width and depth that runs across the protein is probably the binding site for the histone substrate. A model for histone H4 binding by Hat1 is discussed in terms of possible sources of specific lysine recognition by the enzyme. The structure of Hat1 provides a model for the structures of the catalytic domains of a protein superfamily that includes other histone acetyltransferases such as Gcn5 and CBP.
    MeSH term(s) Acetyl Coenzyme A/chemistry ; Acetyltransferases/chemistry ; Acetyltransferases/genetics ; Acetyltransferases/metabolism ; Amino Acid Sequence ; Arylamine N-Acetyltransferase/chemistry ; Binding Sites ; Catalysis ; Crystallography ; DNA-Binding Proteins ; Fungal Proteins/chemistry ; Histone Acetyltransferases ; Histones/metabolism ; Models, Molecular ; Molecular Sequence Data ; Multigene Family ; Protein Conformation ; Protein Kinases/chemistry ; Protein Structure, Secondary ; Recombinant Proteins/chemistry ; Saccharomyces cerevisiae/enzymology ; Saccharomyces cerevisiae Proteins ; Sequence Homology, Amino Acid ; Synchrotrons
    Chemical Substances DNA-Binding Proteins ; Fungal Proteins ; Histones ; Recombinant Proteins ; Saccharomyces cerevisiae Proteins ; Acetyl Coenzyme A (72-89-9) ; Acetyltransferases (EC 2.3.1.-) ; GCN5 protein, S cerevisiae (EC 2.3.1.48) ; Histone Acetyltransferases (EC 2.3.1.48) ; histone acetyltransferase type B complex (EC 2.3.1.48) ; Arylamine N-Acetyltransferase (EC 2.3.1.5) ; Protein Kinases (EC 2.7.-)
    Language English
    Publishing date 1998-08-21
    Publishing country United States
    Document type Comparative Study ; Journal Article ; Research Support, Non-U.S. Gov't ; Research Support, U.S. Gov't, Non-P.H.S. ; Research Support, U.S. Gov't, P.H.S.
    ZDB-ID 187009-9
    ISSN 1097-4172 ; 0092-8674
    ISSN (online) 1097-4172
    ISSN 0092-8674
    DOI 10.1016/s0092-8674(00)81584-6
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    In stock of ZB MED Cologne/Königswinter

    Zs.A 1167: Show issues Location:
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  3. Article: The something about silencing protein, Sas3, is the catalytic subunit of NuA3, a yTAF(II)30-containing HAT complex that interacts with the Spt16 subunit of the yeast CP (Cdc68/Pob3)-FACT complex.

    John, S / Howe, L / Tafrov, S T / Grant, P A / Sternglanz, R / Workman, J L

    Genes & development

    2000  Volume 14, Issue 10, Page(s) 1196–1208

    Abstract: We have purified and characterized a Gcn5-independent nucleosomal histone H3 HAT complex, NuA3 (Nucleosomal Acetyltransferase of histone H3). Peptide sequencing of proteins from the purified NuA3 complex identified Sas3 as the catalytic HAT subunit of ... ...

    Abstract We have purified and characterized a Gcn5-independent nucleosomal histone H3 HAT complex, NuA3 (Nucleosomal Acetyltransferase of histone H3). Peptide sequencing of proteins from the purified NuA3 complex identified Sas3 as the catalytic HAT subunit of the complex. Sas3 is the yeast homolog of the human MOZ oncogene. Sas3 is required for both the HAT activity and the integrity of the NuA3 complex. In addition, NuA3 contains the TBP- associated factor, yTAF(II)30, which is also a component of the TFIID, TFIIF, and SWI/SNF complexes. Sas3 mediates interaction of the NuA3 complex with Spt16 both in vivo and in vitro. Spt16 functions as a component of the yeast CP (Cdc68/Pob3) and mammalian FACT (facilitates chromatin transcription) complexes, which are involved in transcription elongation and DNA replication. This interaction suggests that the NuA3 complex might function in concert with FACT-CP to stimulate transcription or replication elongation through nucleosomes by providing a coupled acetyltransferase activity.
    MeSH term(s) Acetyltransferases/chemistry ; Acetyltransferases/genetics ; Acetyltransferases/isolation & purification ; Acetyltransferases/metabolism ; Amino Acid Sequence ; Binding Sites ; Carrier Proteins/metabolism ; Catalytic Domain ; Cell Cycle Proteins/chemistry ; Cell Cycle Proteins/genetics ; Cell Cycle Proteins/metabolism ; DNA Replication/genetics ; DNA-Binding Proteins/chemistry ; DNA-Binding Proteins/genetics ; DNA-Binding Proteins/isolation & purification ; DNA-Binding Proteins/metabolism ; Fungal Proteins/physiology ; Gene Expression Regulation, Fungal ; HeLa Cells ; Histone Acetyltransferases ; Humans ; Models, Biological ; Molecular Sequence Data ; Molecular Weight ; Multienzyme Complexes/chemistry ; Multienzyme Complexes/genetics ; Multienzyme Complexes/isolation & purification ; Multienzyme Complexes/metabolism ; Mutation/genetics ; Precipitin Tests ; Protein Binding ; Protein Kinases/physiology ; Recombinant Fusion Proteins/chemistry ; Recombinant Fusion Proteins/genetics ; Recombinant Fusion Proteins/isolation & purification ; Recombinant Fusion Proteins/metabolism ; Saccharomyces cerevisiae/enzymology ; Saccharomyces cerevisiae/genetics ; Saccharomyces cerevisiae Proteins ; TATA-Binding Protein Associated Factors ; Transcription Factor TFIID ; Transcription Factors/chemistry ; Transcription Factors/genetics ; Transcription Factors/isolation & purification ; Transcription Factors/metabolism ; Transcription, Genetic/genetics ; Transcriptional Elongation Factors ; Two-Hybrid System Techniques
    Chemical Substances Carrier Proteins ; Cell Cycle Proteins ; DNA-Binding Proteins ; Fungal Proteins ; Multienzyme Complexes ; POB3 protein, S cerevisiae ; Recombinant Fusion Proteins ; SPT16 protein, S cerevisiae ; SUPT16H protein, human ; Saccharomyces cerevisiae Proteins ; TAF10 protein, human ; TATA-Binding Protein Associated Factors ; Transcription Factor TFIID ; Transcription Factors ; Transcriptional Elongation Factors ; Acetyltransferases (EC 2.3.1.-) ; GCN5 protein, S cerevisiae (EC 2.3.1.48) ; Histone Acetyltransferases (EC 2.3.1.48) ; Protein Kinases (EC 2.7.-)
    Language English
    Publishing date 2000-05-15
    Publishing country United States
    Document type Journal Article ; Research Support, Non-U.S. Gov't ; Research Support, U.S. Gov't, P.H.S.
    ZDB-ID 806684-x
    ISSN 1549-5477 ; 0890-9369
    ISSN (online) 1549-5477
    ISSN 0890-9369
    Database MEDical Literature Analysis and Retrieval System OnLINE

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  4. Article: Crystal structure of the histone acetyltransferase Hpa2: A tetrameric member of the Gcn5-related N-acetyltransferase superfamily.

    Angus-Hill, M L / Dutnall, R N / Tafrov, S T / Sternglanz, R / Ramakrishnan, V

    Journal of molecular biology

    1999  Volume 294, Issue 5, Page(s) 1311–1325

    Abstract: We report the crystal structure of the yeast protein Hpa2 in complex with acetyl coenzyme A (AcCoA) at 2.4 A resolution and without cofactor at 2.9 A resolution. Hpa2 is a member of the Gcn5-related N-acetyltransferase (GNAT) superfamily, a family of ... ...

    Abstract We report the crystal structure of the yeast protein Hpa2 in complex with acetyl coenzyme A (AcCoA) at 2.4 A resolution and without cofactor at 2.9 A resolution. Hpa2 is a member of the Gcn5-related N-acetyltransferase (GNAT) superfamily, a family of enzymes with diverse substrates including histones, other proteins, arylalkylamines and aminoglycosides. In vitro, Hpa2 is able to acetylate specific lysine residues of histones H3 and H4 with a preference for Lys14 of histone H3. Hpa2 forms a stable dimer in solution and forms a tetramer upon binding AcCoA. The crystal structure reveals that the Hpa2 tetramer is stabilized by base-pair interactions between the adenine moieties of the bound AcCoA molecules. These base-pairs represent a novel method of stabilizing an oligomeric protein structure. Comparison of the structure of Hpa2 with those of other GNAT superfamily members illustrates a remarkably conserved fold of the catalytic domain of the GNAT family even though members of this family share low levels of sequence homology. This comparison has allowed us to better define the borders of the four sequence motifs that characterize the GNAT family, including a motif that is not discernable in histone acetyltransferases by sequence comparison alone. We discuss implications of the Hpa2 structure for the catalytic mechanism of the GNAT enzymes and the opportunity for multiple histone tail modification created by the tetrameric Hpa2 structure.
    MeSH term(s) Acetyl Coenzyme A/chemistry ; Acetyl Coenzyme A/metabolism ; Acetylation ; Acetyltransferases/chemistry ; Acetyltransferases/metabolism ; Adenine/metabolism ; Amino Acid Motifs ; Amino Acid Sequence ; Base Pairing ; Binding Sites ; Catalytic Domain ; Conserved Sequence ; Crystallization ; Crystallography, X-Ray ; DNA-Binding Proteins ; Dimerization ; Fungal Proteins/chemistry ; Fungal Proteins/metabolism ; Histone Acetyltransferases ; Histones/metabolism ; Models, Molecular ; Molecular Sequence Data ; Multigene Family ; Protein Folding ; Protein Kinases/chemistry ; Protein Kinases/metabolism ; Protein Structure, Quaternary ; Saccharomyces cerevisiae/enzymology ; Saccharomyces cerevisiae Proteins ; Structure-Activity Relationship
    Chemical Substances DNA-Binding Proteins ; Fungal Proteins ; Histones ; Saccharomyces cerevisiae Proteins ; Acetyl Coenzyme A (72-89-9) ; Acetyltransferases (EC 2.3.1.-) ; GCN5 protein, S cerevisiae (EC 2.3.1.48) ; Histone Acetyltransferases (EC 2.3.1.48) ; Protein Kinases (EC 2.7.-) ; Adenine (JAC85A2161)
    Language English
    Publishing date 1999-12-17
    Publishing country England
    Document type Journal Article ; Research Support, U.S. Gov't, Non-P.H.S. ; Research Support, U.S. Gov't, P.H.S.
    ZDB-ID 80229-3
    ISSN 1089-8638 ; 0022-2836
    ISSN (online) 1089-8638
    ISSN 0022-2836
    DOI 10.1006/jmbi.1999.3338
    Database MEDical Literature Analysis and Retrieval System OnLINE

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    In stock of ZB MED Cologne/Königswinter

    Zs.A 867: Show issues Location:
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  5. Article: Crystal structure of the histone acetyltransferase Hpa2: a tetrameric member of the Gcn5-related N-acetyltransferase superfamily

    Angus-Hill, M.L / Dutnall, R.N / Tafrov, S.T / Sternglanz, R / Ramakrishnan, V

    Journal of molecular biology. Dec 17, 1999. v. 294 (5)

    1999  

    Keywords X-ray diffraction ; Saccharomyces cerevisiae ; acyltransferases ; crystals ; molecular conformation ; enzyme activity ; acetylation ; histones ; acetyl coenzyme A
    Language English
    Dates of publication 1999-1217
    Size p. 1311-1325.
    Document type Article
    ZDB-ID 80229-3
    ISSN 1089-8638 ; 0022-2836
    ISSN (online) 1089-8638
    ISSN 0022-2836
    Database NAL-Catalogue (AGRICOLA)

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  6. Article: The silencing protein SIR2 and its homologs are NAD-dependent protein deacetylases.

    Landry, J / Sutton, A / Tafrov, S T / Heller, R C / Stebbins, J / Pillus, L / Sternglanz, R

    Proceedings of the National Academy of Sciences of the United States of America

    2000  Volume 97, Issue 11, Page(s) 5807–5811

    Abstract: Homologs of the chromatin-bound yeast silent information regulator 2 (SIR2) protein are found in organisms from all biological kingdoms. SIR2 itself was originally discovered to influence mating-type control in haploid cells by locus-specific ... ...

    Abstract Homologs of the chromatin-bound yeast silent information regulator 2 (SIR2) protein are found in organisms from all biological kingdoms. SIR2 itself was originally discovered to influence mating-type control in haploid cells by locus-specific transcriptional silencing. Since then, SIR2 and its homologs have been suggested to play additional roles in suppression of recombination, chromosomal stability, metabolic regulation, meiosis, and aging. Considering the far-ranging nature of these functions, a major experimental goal has been to understand the molecular mechanism(s) by which this family of proteins acts. We report here that members of the SIR2 family catalyze an NAD-nicotinamide exchange reaction that requires the presence of acetylated lysines such as those found in the N termini of histones. Significantly, these enzymes also catalyze histone deacetylation in a reaction that absolutely requires NAD, thereby distinguishing them from previously characterized deacetylases. The enzymes are active on histone substrates that have been acetylated by both chromatin assembly-linked and transcription-related acetyltransferases. Contrary to a recent report, we find no evidence that these proteins ADP-ribosylate histones. Discovery of an intrinsic deacetylation activity for the conserved SIR2 family provides a mechanism for modifying histones and other proteins to regulate transcription and diverse biological processes.
    MeSH term(s) Acetylation ; Adenosine Diphosphate Ribose/metabolism ; Animals ; Chickens ; Fungal Proteins/genetics ; Fungal Proteins/physiology ; Gene Silencing/physiology ; Histone Deacetylases/genetics ; Histone Deacetylases/physiology ; Histones/chemistry ; Histones/metabolism ; Lysine/metabolism ; Multigene Family ; NAD/metabolism ; Niacinamide/metabolism ; Protein Processing, Post-Translational ; Recombinant Fusion Proteins/metabolism ; Saccharomyces cerevisiae/enzymology ; Saccharomyces cerevisiae/genetics ; Silent Information Regulator Proteins, Saccharomyces cerevisiae ; Sirtuin 2 ; Sirtuins ; Trans-Activators/genetics ; Trans-Activators/physiology
    Chemical Substances Fungal Proteins ; Histones ; Recombinant Fusion Proteins ; Silent Information Regulator Proteins, Saccharomyces cerevisiae ; Trans-Activators ; NAD (0U46U6E8UK) ; Adenosine Diphosphate Ribose (20762-30-5) ; Niacinamide (25X51I8RD4) ; SIR2 protein, S cerevisiae (EC 3.5.1.-) ; Sirtuin 2 (EC 3.5.1.-) ; Sirtuins (EC 3.5.1.-) ; Histone Deacetylases (EC 3.5.1.98) ; Lysine (K3Z4F929H6)
    Language English
    Publishing date 2000-03-21
    Publishing country United States
    Document type Journal Article ; Research Support, U.S. Gov't, P.H.S.
    ZDB-ID 209104-5
    ISSN 1091-6490 ; 0027-8424
    ISSN (online) 1091-6490
    ISSN 0027-8424
    DOI 10.1073/pnas.110148297
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