The two-domain ribosomal protein L1 is a structural part of L1 stalk in ribosome and a translational repressor of protein synthesis of its own operon. The regulation of the L11 operon Escherichia coli (consists of genes of proteins L11 and L1) and L1 operon of Achaea from Methanococcus (includes genes of proteins L1, L10 and L12) is well-studied. Previously we have shown that domain I of ribosomal protein L1 Thermus thermophilus (TthL1dI) can regulate expression of L1 gene as an intact protein TthL1. Plasmid construct carrying the gene of truncation mutant of L1 from Methanococcus jannaschii was obtained in this study and the isolated domain I of M. jannaschii (MjaL1dI) was overproduced and purified. Kinetic analysis of MjaL1dI interaction with specific 23S rRNA and mRNA fragments was performed by surface plasmon resonance technique. Here it was shown that domain I of archaeal ribosomal protein L1 binds with rRNA with higher affinity than with mRNA as an intact protein L1. In a coupled transcription-translation system E.coli in vitro MjaL1dI inhibits synthesis of ribosomal protein L1. We conclude that MjaL1dI, as a TthL1dI, may have regulatory properties as an intact protein. Thus, these data suggest conservative regulatory properties of the domain I of L1 ribosomal protein as in Bacteria, and in the Archaea.
ribosomal protein L1, regulation of translation, RNA-protein interactions, surface plasmon resonance
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