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Article: Deciphering NAD-dependent deacetylases.

Dutnall, R N / Pillus, L

2001 Volume 105, Issue 2, Page(s) 161–164

MeSH term(s)	Animals ; DNA/genetics ; DNA/metabolism ; Histone Deacetylases/genetics ; Histone Deacetylases/metabolism ; Humans ; Multigene Family/genetics ; NAD/metabolism ; Protein Binding ; Protein Structure, Tertiary ; Substrate Specificity
Chemical Substances	NAD (0U46U6E8UK) ; DNA (9007-49-2) ; Histone Deacetylases (EC 3.5.1.98)
Language	English
Publishing date	2001-04-20
Publishing country	United States
Document type	Comment ; Journal Article ; Review
ZDB-ID	187009-9
ISSN	1097-4172 ; 0092-8674
ISSN (online)	1097-4172
ISSN	0092-8674
DOI	10.1016/s0092-8674(01)00305-1
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Zs.A 1167: Show issues			Location: Je nach Verfügbarkeit (siehe Angabe bei Bestand) bis Jg. 1994: Bestellungen von Artikeln über das Online-Bestellformular Jg. 1995 - 2021: Lesesall (1.OG) ab Jg. 2022: Lesesaal (EG)
Zs.MG 58: Show issues

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Article: Twists and turns of the nucleosome: tails without ends.

Dutnall, R N / Ramakrishnan, V

Structure (London, England : 1993)

1997 Volume 5, Issue 10, Page(s) 1255–1259

Abstract: The high-resolution structure of a nucleosome core particle gives us our first detailed look at the primary level of eukaryotic DNA organization. The structure reveals the nature of histone-DNA contacts and provides some surprises regarding the histone ... ...

Abstract	The high-resolution structure of a nucleosome core particle gives us our first detailed look at the primary level of eukaryotic DNA organization. The structure reveals the nature of histone-DNA contacts and provides some surprises regarding the histone tails and their possible involvement in higher levels of chromatin organization.
MeSH term(s)	Animals ; Base Sequence ; Crystallography, X-Ray ; DNA/chemistry ; Eukaryotic Cells ; Histones/chemistry ; Models, Molecular ; Molecular Sequence Data ; Nucleic Acid Conformation ; Nucleosomes/chemistry ; Protein Conformation
Chemical Substances	Histones ; Nucleosomes ; DNA (9007-49-2)
Language	English
Publishing date	1997-10-15
Publishing country	United States
Document type	Journal Article ; Review
ZDB-ID	1213087-4
ISSN	1878-4186 ; 0969-2126
ISSN (online)	1878-4186
ISSN	0969-2126
DOI	10.1016/s0969-2126(97)00276-1
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Zs.A 4141: Show issues

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Article: Effects of acetylation of histone H4 at lysines 8 and 16 on activity of the Hat1 histone acetyltransferase.

Makowski, A M / Dutnall, R N / Annunziato, A T

The Journal of biological chemistry

2001 Volume 276, Issue 47, Page(s) 43499–43502

Abstract: ... R. N., Tafrov, S. T., Sternglanz, R., and Ramakrishnan, V. (1998) Cell 94, 427-438) and provide ... These results present strong support for the model of H4-Hat1p interaction proposed by Dutnall et al. (Dutnall ...

Abstract	During nucleosome assembly in vivo, newly synthesized histone H4 is specifically diacetylated on lysines 5 and 12 within the H4 NH(2)-terminal tail domain. The highly conserved "K5/K12" deposition pattern of acetylation is thought to be generated by the Hat1 histone acetyltransferase, which in vivo is found in the HAT-B complex. In the following report, the activity and substrate specificity of the human HAT-B complex and of recombinant yeast Hat1p have been examined, using synthetic H4 NH(2)-terminal peptides as substrates. As expected, the unacetylated H4 peptide was a good substrate for acetylation by yeast Hat1p and human HAT-B, while the K5/K12-diacetylated peptide was not significantly acetylated. Notably, an H4 peptide previously diacetylated on lysines 8 and 16 was a very poor substrate for acetylation by either yeast Hat1p or human HAT-B. Treating the K8/K16-diacetylated peptide with histone deacetylase prior to the HAT-B reaction raised acetylation at K5/K12 to 70-80% of control levels. These results present strong support for the model of H4-Hat1p interaction proposed by Dutnall et al. (Dutnall, R. N., Tafrov, S. T., Sternglanz, R., and Ramakrishnan, V. (1998) Cell 94, 427-438) and provide evidence for the first time that site-specific acetylation of histones can regulate the acetylation of other substrate sites.
MeSH term(s)	Acetylation ; Acetyltransferases/chemistry ; Acetyltransferases/metabolism ; HeLa Cells ; Histone Acetyltransferases ; Histones/chemistry ; Histones/metabolism ; Humans ; Lysine/metabolism ; Recombinant Proteins/chemistry ; Recombinant Proteins/metabolism ; Substrate Specificity
Chemical Substances	Histones ; Recombinant Proteins ; Acetyltransferases (EC 2.3.1.-) ; Histone Acetyltransferases (EC 2.3.1.48) ; histone acetyltransferase type B complex (EC 2.3.1.48) ; Lysine (K3Z4F929H6)
Language	English
Publishing date	2001-10-03
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	2997-x
ISSN	1083-351X ; 0021-9258
ISSN (online)	1083-351X
ISSN	0021-9258
DOI	10.1074/jbc.C100549200
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Article: The solution structure of the first zinc finger domain of SWI5: a novel structural extension to a common fold.

Dutnall, R N / Neuhaus, D / Rhodes, D

Structure (London, England : 1993)

1996 Volume 4, Issue 5, Page(s) 599–611

Abstract: ... sequence homology, which extends into a region N-terminal to the first finger, suggesting that the DNA-binding ... of the zinc fingers of SWI5 reveals that a 15 residue region N-terminal to the finger motifs forms part ...

Abstract	Background: The 2Cys-2His (C2-H2) zinc finger is a protein domain commonly used for sequence-specific DNA recognition. The zinc fingers of the yeast transcription factors SWI5 and ACE2 share strong sequence homology, which extends into a region N-terminal to the first finger, suggesting that the DNA-binding domains of these two proteins include additional structural elements. Results: Structural analysis of the zinc fingers of SWI5 reveals that a 15 residue region N-terminal to the finger motifs forms part of the structure of the first finger domain, adding a beta strand and a helix not previously observed in other zinc finger structures. Sequence analysis suggests that other zinc finger proteins may also have this structure. Biochemical studies show that this additional structure increases DNA-binding affinity. Conclusions: The structural analysis presented reveals a novel zinc finger structure in which additional structural elements have been added to the C2-H2 zinc finger fold. This additional structure may enhance stability and has implications for DNA recognition by extending the potential DNA-binding surface of a single zinc finger domain.
MeSH term(s)	Amino Acid Sequence ; Cell Cycle Proteins ; Fungal Proteins/chemistry ; Magnetic Resonance Spectroscopy ; Models, Molecular ; Molecular Sequence Data ; Protein Structure, Tertiary ; Saccharomyces cerevisiae Proteins ; Sequence Alignment ; Sequence Homology, Amino Acid ; Solutions ; Transcription Factors/chemistry ; Zinc Fingers
Chemical Substances	Cell Cycle Proteins ; Fungal Proteins ; SWI5 protein, S cerevisiae ; Saccharomyces cerevisiae Proteins ; Solutions ; Transcription Factors
Language	English
Publishing date	1996-05-15
Publishing country	United States
Document type	Journal Article ; Research Support, Non-U.S. Gov't
ZDB-ID	1213087-4
ISSN	1878-4186 ; 0969-2126
ISSN (online)	1878-4186
ISSN	0969-2126
DOI	10.1016/s0969-2126(96)00064-0
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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
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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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Zs.A 1167: Show issues			Location: Je nach Verfügbarkeit (siehe Angabe bei Bestand) bis Jg. 1994: Bestellungen von Artikeln über das Online-Bestellformular Jg. 1995 - 2021: Lesesall (1.OG) ab Jg. 2022: Lesesaal (EG)
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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: ... at 2.4 A resolution and without cofactor at 2.9 A resolution. Hpa2 is a member of the Gcn5-related N ...

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
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Zs.A 867: Show issues

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Article: The cocrystal structures of two zinc-stabilized DNA-binding domains illustrate different ways of achieving sequence-specific DNA recognition.

Schwabe, J W / Fairall, L / Chapman, L / Finch, J T / Dutnall, R N / Rhodes, D

Cold Spring Harbor symposia on quantitative biology

1993 Volume 58, Page(s) 141–147

MeSH term(s)	Amino Acid Sequence ; Animals ; Base Sequence ; Binding Sites ; Crystallography, X-Ray ; DNA/genetics ; DNA/metabolism ; DNA-Binding Proteins/chemistry ; DNA-Binding Proteins/genetics ; DNA-Binding Proteins/metabolism ; Drosophila ; Drosophila Proteins ; Humans ; Models, Molecular ; Molecular Sequence Data ; Molecular Structure ; Nucleic Acid Conformation ; Protein Conformation ; Receptors, Estrogen/chemistry ; Receptors, Estrogen/genetics ; Receptors, Estrogen/metabolism ; Repressor Proteins ; Transcription Factors/chemistry ; Transcription Factors/genetics ; Transcription Factors/metabolism ; Zinc Fingers/genetics
Chemical Substances	DNA-Binding Proteins ; Drosophila Proteins ; Receptors, Estrogen ; Repressor Proteins ; Transcription Factors ; ttk protein, Drosophila ; DNA (9007-49-2)
Language	English
Publishing date	1993
Publishing country	United States
Document type	Journal Article
ISSN	0091-7451
ISSN	0091-7451
DOI	10.1101/sqb.1993.058.01.018
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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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