CRM domain
| CRS1_YhbY | |||||||||
|---|---|---|---|---|---|---|---|---|---|
 solution structure of the hypothetical protein sav1595 from staphylococcus aureus, a putative rna binding protein | |||||||||
| Identifiers | |||||||||
| Symbol | CRS1_YhbY | ||||||||
| Pfam | PF01985 | ||||||||
| InterPro | IPR001890 | ||||||||
| PROSITE | PDOC01005 | ||||||||
| SCOP2 | 1jo0/SCOPe/SUPFAM | ||||||||
| |||||||||
In molecular biology, theCRM domainis an approximately 100-amino acidRNA-binding domain. The name CRM (chloroplastRNAsplicingandribosomematuration) has been suggested to reflect the functions established for four characterised members of the family:Zea mays(Maize) CRS1, CAF1 and CAF2proteinsand theEscherichia coliprotein YhbY. Proteins containing the CRM domain are found ineubacteria,archaea,andplants.The CRM domain is represented as a stand-alone protein inarchaeaand bacteria, and in single- and multi-domainproteinsinplants.It has been suggested thatprokaryoticCRMproteinsexisted as ribosome-associated proteins prior to the divergence of archaea and bacteria, and that they were co-opted in the plant lineage as RNAbindingmodules by incorporation into diverse protein contexts. Plant CRMdomainsare predicted to reside not only in the chloroplast, but also in themitochondrionand the nucleo/cytoplasmic compartment. The diversity of the CRM domain family in plants suggests a diverse set of RNA targets.[1][2]
The CRM domain is a compact alpha/beta domain consisting of a four-strandedbeta sheetand threealpha heliceswith an alpha-beta-alpha-beta-alpha-beta-beta topology. The beta sheet face is basic, consistent with a role in RNA binding. Proximal to the basic beta sheet face is another moiety that could contribute tonucleic acidrecognition. Connecting strand beta1 andhelixalpha2 is aloopwith a sixamino acidmotif, GxxG flanked by largealiphaticresidues, within which one 'x' is typically abasicresidue.[3]
Escherichia coliYhbY is associated with pre-50Sribosomalsubunits, which implies a function in ribosome assembly.GFPfused to a single-domain CRM protein frommaizelocalises to thenucleolus,suggesting that an analogous activity may have been retained in plants.[2]A CRM domain containing protein in plant chloroplasts has been shown to function in group I and IIintronsplicing.[4]In vitroexperiments with an isolated maize CRM domain have shown it to have RNA binding activity. These and other results suggest that the CRM domainevolvedin 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 theevolutionof plantgenomes.[2]YhbY has afoldsimilar to that of the C-terminal domain oftranslationinitiation factor3 (IF3C), whichbindsto 16S rRNA in the 30S ribosome.[5]
References
[edit]- ^Ostheimer GJ, Williams-Carrier R, Belcher S, Osborne E, Gierke J, Barkan A (August 2003)."Group II intron splicing factors derived by diversification of an ancient RNA-binding domain".EMBO J.22(15): 3919–29.doi:10.1093/emboj/cdg372.PMC169045.PMID12881426.
- ^abcBarkan A, Klipcan L, Ostersetzer O, Kawamura T, Asakura Y, Watkins KP (January 2007)."The CRM domain: an RNA binding module derived from an ancient ribosome-associated protein".RNA.13(1): 55–64.doi:10.1261/rna.139607.PMC1705760.PMID17105995.
- ^Ostheimer GJ, Barkan A, Matthews BW (November 2002)."Crystal structure of E. coli YhbY: a representative of a novel class of RNA binding proteins".Structure.10(11): 1593–601.doi:10.1016/S0969-2126(02)00886-9.PMID12429100.
- ^Asakura Y, Barkan A (December 2007)."A CRM domain protein functions dually in group I and group II intron splicing in land plant chloroplasts".Plant Cell.19(12): 3864–75.doi:10.1105/tpc.107.055160.PMC2217638.PMID18065687.
- ^Till B, Schmitz-Linneweber C, Williams-Carrier R, Barkan A (September 2001)."CRS1 is a novel group II intron splicing factor that was derived from a domain of ancient origin".RNA.7(9): 1227–38.doi:10.1017/S1355838201010445.PMC1370168.PMID11565746.