Solution structure of the carboxy-terminal Tudor domain from human Coilin.
The Cajal body is a dynamic eukaryotic nuclear organelle that is known primarily as an organizational center for the assembly of snRNAs involved in transcript splicing. One of the most critical components of the Cajal body is the scaffolding protein, Coilin. Here, we demonstrate by NMR methods that the carboxy-terminal region contains a Tudor domain. The Tudor domain is atypical due to the presence of several unstructured loops, one greater than thirty amino acids in length. Tudor domains have been noted previously to bind DNA, RNA and modified amino acids. The absence of these sequence and structural signatures in the Coilin Tudor domain supporting these established functions suggests an alternative role.
Shanbhag
Riya
R
Department of Biology, York University, Toronto, ON, Canada.
Kurabi
Arwa
A
Kwan
Jamie J
JJ
Donaldson
Logan W
LW
D000595:Amino Acid Sequence; D001665:Binding Sites / Q000235:genetics; D002942:Circular Dichroism; D006801:Humans; D009682:Magnetic Resonance Spectroscopy / Q000379:methods; D008958:Models, Molecular; D008969:Molecular Sequence Data; D009687:Nuclear Proteins / Q000737:chemistry* / Q000235:genetics / Q000378:metabolism; D017433:Protein Structure, Secondary; D017434:Protein Structure, Tertiary; D017386:Sequence Homology, Amino Acid; D012996:Solutions
D009687:Nuclear Proteins; D012996:Solutions; C068921:p80-coilin