Laboratory for Structural Studies of the Translation Apparatus

The Laboratory was founded in the 1980s. 

The first Head of the Laboratory was Prof. Dr. Maria Garber.

From 2016 the Head of the Laboratory is Dr. Sc. Alexey Nikulin.

Brief history of the laboratory.

The substantial history of the laboratory begins from obtaining crystals of elongation factors EF-G and crystals of the 70S ribosome and 30S ribosomal subunit from an extremely thermophilic bacterium Thermus thermophilus. Data on ribosome crystals formed the basis for the main work of a number of international laboratories on measuring the structure of 70S ribosomes and 30S ribosomal subunits of T. thermophilus, which were awarded the Nobel Prize in Chemistry in 2009

In the 90s, together with the Group for Structural Studies of Ribosomal Proteins and in collaboration with colleagues from Sweden, Austria and France, the structures of a number of ribosomal proteins and their complexes with specific fragments of ribosomal RNA were determined. The structures of five complexes of various ribosomal proteins with rRNA have been actively used to clarify the structures of bacterial ribosomal subunits.

In 2000s, we have studied translation initiation factor 2 from archaea. It is a heterotrimeric protein homologous in archaea and eukaryotes (a/eIF2). We have determined for the first time the structure of full-length aIF2 and the structure of the functionally important ternary complex of this protein with GTP and methionylated initiator tRNA. Together with the group of I. Shatsky (MSU), it was shown that the archaeal factor aIF2 is capable of forming a preinitiation complex with the eukaryotic ribosome.

An important object of research was the bacterial regulator of the translation of many genes, the Hfq protein. Its structure from the bacterium Pseudomonas aeruginosa, the structure of its complexes with ribonucleotides were determined, and the structure of the functionally important lateral RNA-binding site of the protein was described. Subsequently, the RNA-binding properties of the Hfq archaeal homologs called SmAP were studied. It was shown that the uridine-binding site of these proteins is universally conserved, and their affinity for poly(U) RNA is higher than that of the Hfq protein. At the same time, SmAP proteins are not able to bind poly(A) RNA, which demonstrates the functional differences between archaeal SmAP proteins and their bacterial homologues.

Current research

Structural and functional studies of proteins and RNA(DNA)-protein complexes, including:

  • Bacterial ribosome maturation and influence of various protein factor on this process (in part of Russian Scientific Foundation grant #19-74-20186).
  • Identification of LepA-dependent mRNAs using selective ribosomal profiling to determine the function of the ribosome-dependent GTPase LepA in bacteria (Russian Scientific Foundation grant #24-24-00396).
  • Structures and functions of RNA-chaperones in pathogen bacteria (Russian Scientific Foundation grant #24-24-00071)
  • Structural investigations of T5 phage, processing and self-assembling of T5 head (in part of Russian Scientific Foundation grant #23-24-00510).
  • Susceptibility factor eIF4E: mutations rational design and obtaining of potato virus Y resistant plants (Russian Scientific Foundation grant #24-44-04007).