A new human member of the MYST family of histone acetyl transferases with high sequence similarity to Drosophila MOF

Karama C. Neal; Antonio Pannuti; Edwin R. Smith; John C. Lucchesi

doi:10.1016/S0167-4781(99)00211-0

A new human member of the MYST family of histone acetyl transferases with high sequence similarity to Drosophila MOF

Karama C. Neal, Antonio Pannuti, Edwin R. Smith, John C. Lucchesi^*

^*Corresponding author for this work

Biochemistry and Molecular Genetics

Research output: Contribution to journal › Article › peer-review

72 Scopus citations

Abstract

We have identified a novel human gene product, hMOF, which exhibits significant similarity to the Drosophila dosage compensation regulator, MOF. A recombinant C-terminal portion of hMOF has histone acetyltransferase activity directed toward histones H3, H2A and H4, a specificity characteristic of other MYST family histone acetyltransferases. Based on hMOF's chromodomain, we discuss possible interactions with other proteins. (C) 2000 Elsevier Science B.V.

Original language	English (US)
Pages (from-to)	170-174
Number of pages	5
Journal	Biochimica et Biophysica Acta - Gene Structure and Expression
Volume	1490
Issue number	1-2
DOIs	https://doi.org/10.1016/S0167-4781(99)00211-0
State	Published - Jan 31 2000

Funding

We wish to thank the members of the Lucchesi laboratory for valuable discussion. K.C.N. was supported by NIH Minority Predoctoral Fellowship (GM18038). This work was supported by a grant from the NIH (GM15691) to J.C.L.

Keywords

Chomodomain
Histone acetyltransferase
MSL3 family
MYST family

ASJC Scopus subject areas

Genetics
Structural Biology
Biophysics
Biochemistry

Access to Document

10.1016/S0167-4781(99)00211-0

Cite this

@article{cbbe226178f34a22a47f88221bcd37e8,

title = "A new human member of the MYST family of histone acetyl transferases with high sequence similarity to Drosophila MOF",

abstract = "We have identified a novel human gene product, hMOF, which exhibits significant similarity to the Drosophila dosage compensation regulator, MOF. A recombinant C-terminal portion of hMOF has histone acetyltransferase activity directed toward histones H3, H2A and H4, a specificity characteristic of other MYST family histone acetyltransferases. Based on hMOF's chromodomain, we discuss possible interactions with other proteins. (C) 2000 Elsevier Science B.V.",

keywords = "Chomodomain, Histone acetyltransferase, MSL3 family, MYST family",

author = "Neal, {Karama C.} and Antonio Pannuti and Smith, {Edwin R.} and Lucchesi, {John C.}",

note = "Funding Information: We wish to thank the members of the Lucchesi laboratory for valuable discussion. K.C.N. was supported by NIH Minority Predoctoral Fellowship (GM18038). This work was supported by a grant from the NIH (GM15691) to J.C.L.",

year = "2000",

month = jan,

day = "31",

doi = "10.1016/S0167-4781(99)00211-0",

language = "English (US)",

volume = "1490",

pages = "170--174",

journal = "Biochimica et Biophysica Acta - Gene Structure and Expression",

issn = "0167-4781",

publisher = "Elsevier B.V.",

number = "1-2",

}

TY - JOUR

T1 - A new human member of the MYST family of histone acetyl transferases with high sequence similarity to Drosophila MOF

AU - Neal, Karama C.

AU - Pannuti, Antonio

AU - Smith, Edwin R.

AU - Lucchesi, John C.

N1 - Funding Information: We wish to thank the members of the Lucchesi laboratory for valuable discussion. K.C.N. was supported by NIH Minority Predoctoral Fellowship (GM18038). This work was supported by a grant from the NIH (GM15691) to J.C.L.

PY - 2000/1/31

Y1 - 2000/1/31

N2 - We have identified a novel human gene product, hMOF, which exhibits significant similarity to the Drosophila dosage compensation regulator, MOF. A recombinant C-terminal portion of hMOF has histone acetyltransferase activity directed toward histones H3, H2A and H4, a specificity characteristic of other MYST family histone acetyltransferases. Based on hMOF's chromodomain, we discuss possible interactions with other proteins. (C) 2000 Elsevier Science B.V.

AB - We have identified a novel human gene product, hMOF, which exhibits significant similarity to the Drosophila dosage compensation regulator, MOF. A recombinant C-terminal portion of hMOF has histone acetyltransferase activity directed toward histones H3, H2A and H4, a specificity characteristic of other MYST family histone acetyltransferases. Based on hMOF's chromodomain, we discuss possible interactions with other proteins. (C) 2000 Elsevier Science B.V.

KW - Chomodomain

KW - Histone acetyltransferase

KW - MSL3 family

KW - MYST family

UR - http://www.scopus.com/inward/record.url?scp=0033973262&partnerID=8YFLogxK

UR - http://www.scopus.com/inward/citedby.url?scp=0033973262&partnerID=8YFLogxK

U2 - 10.1016/S0167-4781(99)00211-0

DO - 10.1016/S0167-4781(99)00211-0

M3 - Article

C2 - 10786633

AN - SCOPUS:0033973262

SN - 0167-4781

VL - 1490

SP - 170

EP - 174

JO - Biochimica et Biophysica Acta - Gene Structure and Expression

JF - Biochimica et Biophysica Acta - Gene Structure and Expression

IS - 1-2

ER -

A new human member of the MYST family of histone acetyl transferases with high sequence similarity to Drosophila MOF

Abstract

Funding

Keywords

ASJC Scopus subject areas

Access to Document

Other files and links

Fingerprint

Cite this