Mammalian protein arginine methyltransferase 7 (PRMT7) specifically targets RXR sites in lysine- and arginine-rich regions

You Feng; Ranjan Maity; Julian P. Whitelegge; Andrea Hadjikyriacou; Ziwei Li; Cecilia Zurita-Lopez; Qais Al-Hadid; Amander T. Clark; Mark T. Bedford; Jean Yves Masson; Steven G. Clarke

doi:10.1074/jbc.M113.525345

Mammalian protein arginine methyltransferase 7 (PRMT7) specifically targets RXR sites in lysine- and arginine-rich regions

You Feng
, Ranjan Maity
, Julian P. Whitelegge
, Andrea Hadjikyriacou
, Ziwei Li
, Cecilia Zurita-Lopez
, Qais Al-Hadid
, Amander T. Clark
, Mark T. Bedford
, Jean Yves Masson
, Steven G. Clarke

Epigenetics & Molecular Carcinogenesis

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

156 Scopus citations

Abstract

Background: Protein arginine methyltransferase 7 (PRMT7) is associated with various functions and diseases, but its substrate specificity is poorly defined. Results: Insect cell-expressed PRMT7 forms ω-monomethylarginine residues at basic RXR sequences in peptides and histone H2B. Conclusion: PRMT7 is a type III PRMT with a unique substrate specificity. Significance: Novel post-translational modification sites generated by PRMT7 may regulate biological function.

Original language	English (US)
Pages (from-to)	37010-37025
Number of pages	16
Journal	Journal of Biological Chemistry
Volume	288
Issue number	52
DOIs	https://doi.org/10.1074/jbc.M113.525345
State	Published - Dec 27 2013

ASJC Scopus subject areas

Biochemistry
Molecular Biology
Cell Biology

Access to Document

10.1074/jbc.M113.525345

Cite this

Feng, Y., Maity, R., Whitelegge, J. P., Hadjikyriacou, A., Li, Z., Zurita-Lopez, C., Al-Hadid, Q., Clark, A. T., Bedford, M. T., Masson, J. Y., & Clarke, S. G. (2013). Mammalian protein arginine methyltransferase 7 (PRMT7) specifically targets RXR sites in lysine- and arginine-rich regions. Journal of Biological Chemistry, 288(52), 37010-37025. https://doi.org/10.1074/jbc.M113.525345

Feng, Y, Maity, R, Whitelegge, JP, Hadjikyriacou, A, Li, Z, Zurita-Lopez, C, Al-Hadid, Q, Clark, AT, Bedford, MT, Masson, JY & Clarke, SG 2013, 'Mammalian protein arginine methyltransferase 7 (PRMT7) specifically targets RXR sites in lysine- and arginine-rich regions', Journal of Biological Chemistry, vol. 288, no. 52, pp. 37010-37025. https://doi.org/10.1074/jbc.M113.525345

@article{03cddda7c8d047c881b84b7c5b17fae3,

title = "Mammalian protein arginine methyltransferase 7 (PRMT7) specifically targets RXR sites in lysine- and arginine-rich regions",

abstract = "Background: Protein arginine methyltransferase 7 (PRMT7) is associated with various functions and diseases, but its substrate specificity is poorly defined. Results: Insect cell-expressed PRMT7 forms ω-monomethylarginine residues at basic RXR sequences in peptides and histone H2B. Conclusion: PRMT7 is a type III PRMT with a unique substrate specificity. Significance: Novel post-translational modification sites generated by PRMT7 may regulate biological function.",

author = "You Feng and Ranjan Maity and Whitelegge, \{Julian P.\} and Andrea Hadjikyriacou and Ziwei Li and Cecilia Zurita-Lopez and Qais Al-Hadid and Clark, \{Amander T.\} and Bedford, \{Mark T.\} and Masson, \{Jean Yves\} and Clarke, \{Steven G.\}",

year = "2013",

month = dec,

day = "27",

doi = "10.1074/jbc.M113.525345",

language = "English (US)",

volume = "288",

pages = "37010--37025",

journal = "Journal of Biological Chemistry",

issn = "0021-9258",

publisher = "American Society for Biochemistry and Molecular Biology Inc.",

number = "52",

}

TY - JOUR

T1 - Mammalian protein arginine methyltransferase 7 (PRMT7) specifically targets RXR sites in lysine- and arginine-rich regions

AU - Feng, You

AU - Maity, Ranjan

AU - Whitelegge, Julian P.

AU - Hadjikyriacou, Andrea

AU - Li, Ziwei

AU - Zurita-Lopez, Cecilia

AU - Al-Hadid, Qais

AU - Clark, Amander T.

AU - Bedford, Mark T.

AU - Masson, Jean Yves

AU - Clarke, Steven G.

PY - 2013/12/27

Y1 - 2013/12/27

N2 - Background: Protein arginine methyltransferase 7 (PRMT7) is associated with various functions and diseases, but its substrate specificity is poorly defined. Results: Insect cell-expressed PRMT7 forms ω-monomethylarginine residues at basic RXR sequences in peptides and histone H2B. Conclusion: PRMT7 is a type III PRMT with a unique substrate specificity. Significance: Novel post-translational modification sites generated by PRMT7 may regulate biological function.

AB - Background: Protein arginine methyltransferase 7 (PRMT7) is associated with various functions and diseases, but its substrate specificity is poorly defined. Results: Insect cell-expressed PRMT7 forms ω-monomethylarginine residues at basic RXR sequences in peptides and histone H2B. Conclusion: PRMT7 is a type III PRMT with a unique substrate specificity. Significance: Novel post-translational modification sites generated by PRMT7 may regulate biological function.

UR - https://www.scopus.com/pages/publications/84891408825

UR - https://www.scopus.com/pages/publications/84891408825#tab=citedBy

U2 - 10.1074/jbc.M113.525345

DO - 10.1074/jbc.M113.525345

M3 - Article

C2 - 24247247

AN - SCOPUS:84891408825

SN - 0021-9258

VL - 288

SP - 37010

EP - 37025

JO - Journal of Biological Chemistry

JF - Journal of Biological Chemistry

IS - 52

ER -

Mammalian protein arginine methyltransferase 7 (PRMT7) specifically targets RXR sites in lysine- and arginine-rich regions

Abstract

ASJC Scopus subject areas

Access to Document

Other files and links

Fingerprint

Cite this