| First Author | Wolffe AP | Year | 1994 |
| Journal | Bioessays | Volume | 16 |
| Issue | 4 | Pages | 245-51 |
| PubMed ID | 8031301 | Mgi Jnum | J:17827 |
| Mgi Id | MGI:65854 | Doi | 10.1002/bies.950160407 |
| Citation | Wolffe AP (1994) Structural and functional properties of the evolutionarily ancient Y-box family of nucleic acid binding proteins. Bioessays 16(4):245-51 |
| abstractText | The Y-box proteins are the most evolutionarily conserved nucleic acid binding proteins yet defined in bacteria, plants and animals. The central nucleic acid binding domain of the vertebrate proteins is 43% identical to a 70-amino-acid-long protein (CS7.4) from E. coli. The structure of this domain consists of an antiparallel five-stranded beta-barrel that recognizes both DNA and RNA. The diverse biological roles of these Y-box proteins range from the control of the E. coli cold-shock stress response to the translational masking of messenger RNA in vertebrate gametes. This review discusses the organization of the prokaryotic and eukaryotic Y-box proteins, how they interact with nucleic acids, and their biological roles, both proven and potential. |
