The ribosomal protein L1 of the Escherichia coli is the regulator of its own L11 operon. The L1 protein binds to the specific site of its own mRNA and repress the translation if there is a deficiency of ribosomal 23S RNA. Regulatory properties of the L1 protein in other bacteria have been poorly studied. This paper examines the affinity of the ribosomal protein L1 from Thermatoga maritima to the specific fragment of mRNA. Analysis of the L11 operon sequences of T. maritima showed that the potential L1 protein binding site is located in the leader sequence of the mRNA of the L11 protein, as in E. coli . Previously, we have shown that the regulatory properties of the whole L1 protein can have its domain I. By the method of microscale thermophoresis we determined the kinetic constants of the interaction of the protein L1 T. maritima (TmaL1) and its domain I (TmaL1Id) with the fragment of the T. maritima mRNA. It is shown that TmaL1 and TmaL1dI specifically interact with the fragment of mRNA, that may suggests the conservative regulatory properties of both the whole L1 protein and its domain I in bacteria.
ribosomal protein L1, Thermatoga maritima, regulation of translation, RNA-protein interactions, micro scale thermophoresis, dynamical light scattering
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