Poly(A) tail synthesis and regulation: recent structural insights.
Polyadenylation at the 3' ends of mRNAs is critical to the translation and stability of the messages. Recently determined structures of poly(A) polymerase, U1A and domains of the poly(A)-binding protein provide a framework for understanding the synthesis and regulation of the poly(A) tail.
Hall
Traci M Tanaka
TM
Laboratory of Structural Biology, National Institute of Environmental Health Sciences, National Institutes of Health, PO Box 12233, MDF3-05, Research Triangle Park, NC 27709, USA. hall4@niehs.nih.gov
D000818:Animals; D029968:Escherichia coli Proteins; D006801:Humans; D009690:Nucleic Acid Conformation; D011061:Poly A / Q000096:biosynthesis* / Q000737:chemistry; D039102:Poly(A)-Binding Proteins; D011062:Polynucleotide Adenylyltransferase / Q000037:antagonists & inhibitors / Q000378:metabolism / Q000502:physiology; D011487:Protein Conformation; D012333:RNA, Messenger / Q000096:biosynthesis* / Q000737:chemistry; D016601:RNA-Binding Proteins / Q000737:chemistry / Q000502:physiology; D017412:Ribonucleoprotein, U1 Small Nuclear / Q000737:chemistry / Q000502:physiology; D013329:Structure-Activity Relationship; D015003:Yeasts
D029968:Escherichia coli Proteins; D039102:Poly(A)-Binding Proteins; D012333:RNA, Messenger; D016601:RNA-Binding Proteins; D017412:Ribonucleoprotein, U1 Small Nuclear; C075339:U1A protein; D011061:Poly A; D011062:Polynucleotide Adenylyltransferase; C063643:pcnB protein, E coli