TY - JOUR
T1 - 4 Structure of protein arginine methyltransferases
AU - Zhang, Xing
AU - Cheng, Xiaodong
N1 - Funding Information:
Work in our laboratories was supported in part by a grant from the National Institute of Health (GM61355). The authors are currently supported by a grant from NIH (GM068680), and Xiaodong Cheng is a Georgia Research Alliance Eminent Scholar.
PY - 2006
Y1 - 2006
N2 - With genome sequencing nearing completion for the modelorganisms used in biomedical research, there is a rapidly growing appreciation that proteomics (including the study of covalent modification to proteins) and transcriptional regulation will likely dominate the research headlines in the next decade. Protein methylation plays a central role in both of these fields, as several different residues (Arg, Lys, Gln) are methylated in cells and methylation plays a central role in regulating chromatin structure and impacts transcription. In some cases, a single arginine can be mono-, symmetrically di-, or asymmetrically di-methylated, with different functional consequences for each of the three forms. This review summarizes the progress that has been made in structural studies of protein arginine methyltrans-ferases and their related sequence conservations; it also discusses, somewhat speculatively, their mechanisms.
AB - With genome sequencing nearing completion for the modelorganisms used in biomedical research, there is a rapidly growing appreciation that proteomics (including the study of covalent modification to proteins) and transcriptional regulation will likely dominate the research headlines in the next decade. Protein methylation plays a central role in both of these fields, as several different residues (Arg, Lys, Gln) are methylated in cells and methylation plays a central role in regulating chromatin structure and impacts transcription. In some cases, a single arginine can be mono-, symmetrically di-, or asymmetrically di-methylated, with different functional consequences for each of the three forms. This review summarizes the progress that has been made in structural studies of protein arginine methyltrans-ferases and their related sequence conservations; it also discusses, somewhat speculatively, their mechanisms.
UR - http://www.scopus.com/inward/record.url?scp=77956698509&partnerID=8YFLogxK
UR - http://www.scopus.com/inward/citedby.url?scp=77956698509&partnerID=8YFLogxK
U2 - 10.1016/S1874-6047(06)80006-5
DO - 10.1016/S1874-6047(06)80006-5
M3 - Article
C2 - 26718038
AN - SCOPUS:77956698509
SN - 1874-6047
VL - 24
SP - 105
EP - 121
JO - Enzymes
JF - Enzymes
IS - C
ER -