Superexpression of the gene encoding the ribosomal protein L1 of Thermus thermophilus and crystallization of its recombinant product
- Institute of Protein, Moscow (Russian Federation); and others
L1 is an RNA-binding core proteins of the ribosome large subunit and is one of the largest ribosomal proteins (25 kDa). L1 of E. coli binds ribosome large subunit RNAs from various organisms due to the conserved nature of both the L1-binding site of rRNA and the RNA-binding site of L1. L1 is a repressor of its own translation and of the translation of L11 ribosomal protein, the gene of which is located on the same operon. In 1990, we crystallized L1 protein from Thermus thermophilus ribosomes. However, X-ray diffraction studies were complicated because of the difficulties in obtaining isomorphous heavy-atom crystal derivatives. For this reason, we cloned the gene coding for L1 protein and obtained its modified forms containing cysteine. In this work, we expressed Th. thermophilus L1 protein in E. coli, obtained its cysteine-containing forms, and isolated and crystallized the recombinant protein. 9 refs., 1 fig.
- OSTI ID:
- 283135
- Journal Information:
- Doklady Biochemistry, Vol. 345; Other Information: PBD: Nov-Dec 1995; TN: Translated from Doklady Akademii Nauk; 345: No. 1, 114-115(1995)
- Country of Publication:
- United States
- Language:
- English
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