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YhbY family RNA-binding protein
Escherichia coli YhbY is associated with pre-50S ribosomal subunits, which implies a function in ribosome assembly. GFP fused to a single-domain CRM protein from maize localises to the nucleolus, suggesting that an analogous activity may have been retained in plants [4]. A CRM domain containing protein in plant chloroplasts has been shown to function in group I and II intron splicing [5]. In vitro experiments with an isolated maize CRM domain have shown it to have RNA binding activity. These and other results suggest that the CRM domain evolved in the context of ribosome function prior to the divergence of Archaea and Bacteria, that this function has been maintained in extant prokaryotes, and that the domain was recruited to serve as an RNA binding module during the evolution of plant genomes [4]. YhbY has a fold similar to that of the C-terminal domain of translation initiation factor 3 (IF3C), which binds to 16S rRNA in the 30S ribosome [1][2]. [1]. 12429100. Crystal structure of E. coli YhbY: a representative of a novel class of RNA binding proteins. Ostheimer GJ, Barkan A, Matthews BW;. Structure (Camb) 2002;10:1593-1601. [2]. 12360533. Structure of HI1333 (YhbY), a putative RNA-binding protein from Haemophilus influenzae. Willis MA, Krajewski W, Chalamasetty VR, Reddy P, Howard A, Herzberg O;. Proteins 2002;49:423-426. [3]. 11565746. CRS1 is a novel group II intron splicing factor that was derived from a domain of ancient origin. Till B, Schmitz-Linneweber C, Williams-Carrier R, Barkan A;. RNA 2001;7:1227-1238. [4]. 17105995. The CRM domain: an RNA binding module derived from an ancient ribosome-associa. TRUNCATED at 1650 bytes (from Pfam)
YhbY family RNA-binding protein similar to ribosome assembly RNA-binding protein YhbY that adopts a fold resembling that of the C-terminal domain of translation initiation factor 3 (IF3C), which binds to 16S rRNA in the 30S ribosome
ribosome assembly RNA-binding protein YhbY
A combination of crystal structure, molecular modeling, and bioinformatic data together suggest that members of this family, including YhbY of E. coli, are RNA binding proteins.
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