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Structural and functional properties of the evolutionarily ancient Y‐box family of nucleic acid binding proteins
Abstract
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 fivestranded β‐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.
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Cited by
Moss, E. G., Lee, R. C., & Ambros, V. (1997) · Cell · doi:10.1016/s0092-8674(00)81906-6 · Cited by 850
A superfamily of proteins that contain the cold-shock domain
Graumann, P. L., & Marahiel, M. A. (1998) · Trends in Biochemical Sciences · doi:10.1016/s0968-0004(98)01255-9 · Cited by 438
Large-scale identification of protein–protein interaction of Escherichia coli K-12
Arifuzzaman, M., Maeda, M., Itoh, A., Nishikata, K., Takita, C., Saito, R., Ara, T., Nakahigashi, K., Huang, H.-C., Hirai, A., et al. (2006) · Genome Research · doi:10.1101/gr.4527806 · Cited by 403
Escherichia coli CspA-family RNA chaperones are transcription antiterminators
Bae, W., Xia, B., Inouye, M., & Severinov, K. (2000) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.97.14.7784 · Cited by 386
Moss, E. G., & Tang, L. (2003) · Developmental Biology · doi:10.1016/s0012-1606(03)00126-x · Cited by 328
Metadata
- Authors
- Wolffe, A. P.
- Venue
- BioEssays
- Publisher
- Wiley
- Published
- 1994-04
- Volume
- 16
- Issue
- 4
- Pages
- 245-251
- ISSN
- 0265-9247 (ISSN-L)
- 1521-1878
- OpenAlex
- W2000608709
- Cited by
- 381
- References
- 0
- FWCI
- 3.85
- Type
- journal article
- Language
- en
- Open access
- closed
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