We are deeply saddened by the passing of Amos Bairoch (1957–2025), the creator of PROSITE. We wish to dedicate our latest paper, published shortly before his death, to him. He will always be a source of inspiration to us.
Our deepest condolences go out to his family and friends, and to all those who had the privilege of working with him. Rest in peace, Amos. Your work will live on long after you are gone.
Our deepest condolences go out to his family and friends, and to all those who had the privilege of working with him. Rest in peace, Amos. Your work will live on long after you are gone.
PROSITE documentation PDOC00922Ribosomal protein L1 signature
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PURL: https://purl.expasy.org/prosite/documentation/PDOC00922
Description
Ribosomal protein L1 is the largest protein from the large ribosomal subunit. In Escherichia coli, L1 is known to bind to the 23S rRNA. It belongs to a family of ribosomal proteins which, on the basis of sequence similarities [1,2], groups:
- Eubacterial L1.
- Algal and plant chloroplast L1.
- Cyanelle L1.
- Archaebacterial L1.
- Vertebrate L10A.
- Yeast SSM1.
As a signature pattern, we selected the best conserved region located in the central section of these proteins. It is located at the end of an α helix thought to be involved in RNA-binding.
Last update:December 2004 / Pattern and text revised.
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Technical section
PROSITE method (with tools and information) covered by this documentation:
References
| 1 | Authors | Nikonov S. Nevskaya N. Eliseikina I. Fomenkova N. Nikulin A. Ossina N. Garber M. Jonsson B.-H. Briand C. Al-Karadaghi S. Svensson A. Aevarsson A. Liljas A. |
| Title | Crystal structure of the RNA binding ribosomal protein L1 from Thermus thermophilus. | |
| Source | EMBO J. 15:1350-1359(1996). | |
| PubMed ID | 8635468 |
| 2 | Authors | Olvera J. Wool I.G. |
| Title | The primary structure of rat ribosomal protein L10a. | |
| Source | Biochem. Biophys. Res. Commun. 220:954-957(1996). | |
| PubMed ID | 8607874 |
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