RNA-Binding Properties of Ribosomal Protein L1 from Thermus thermophilus

I. A. Eliseikina,¹ N. K. Avliyakulov,¹ I. B. Grishkovskaya,¹ T. A. Muranova,² S. E. Sedelnikova,¹ and M. B. Garber^1,3

¹Institute of Protein Research, Russian Academy of Sciences, Pushchino, Moscow Region, 142292 Russia; fax: (7-095) 924-04-93; E-mail: protres@sovam.com; garber@vax.ipr.serpukhov.su

²Branch of Shemyakin and Ovchinnikov Institute of Bioorganic Chemistry, Pushchino, Moscow Region, 142292 Russia; fax: (7-095) 925-23-42; E-mail: biochem@sovamsu.sovusa.com

³To whom correspondence should be addressed.

Submitted June 18, 1996; revision submitted July 16, 1996.

Several proteolytic fragments of ribosomal protein L1 from Thermus thermophilus were obtained. The binding of intact protein L1 and its proteolytic fragments to 23S ribosomal RNA has been studied. The first eight N-terminal amino acid residues of the protein are important for the RNA binding; removal of these acids results in a significant decrease in the RNA-binding capacity of protein L1. Cleavage of the polypeptide chain between residues 36 and 37 completely abolishes the RNA binding. Comparison of the data obtained from the recently determined spatial structure of protein L1 clarifies the nature of the interactions that control specific and strong association of protein L1 with 23S rRNA.

KEY WORDS: RNA-protein interaction, ribosomal protein L1, Thermus thermophilus, limited proteolysis.

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