Metlitskaya Anastasia Zusievna | Institute of Molecular Genetics
Academic degree:
Doctor of Philosophy (Biology)

Academic title:
without academic rank


Division of IMG:
Laboratory of gene expression regulation of mobile elements of prokaryotes

Position:
Senior Researcher


Telephone:
+7-499-196-02-03

Е-mail:
azmetlitskaya@gmail.com



Main research interests

The main publications relate to  investigations of  microcin C Microcin C (McC), the smallest microcin known, is produced by Escherichia coli cells harboring a plasmid-borne gene cluster.Mature McC (Mw = 1178 Da) is a heptapeptide with covalently attached С-terminal adenosine monophosphate and a propylamine group attached to the phosphate McC enters susceptible E. coli cells through the YejABEF inner-membrane transporter . Inside the cell, the peptide part is processed by intracellular aminopeptidases (9) to release processed McC—a non-hydrolysable analog of aspartyl-adenylate, which specifically inhibits aspartyl-tRNA synthetase (Asp-RS), leading to cessation of translation.


Publications

  1. The molecular mechanism of aminopropylation of peptide-nucleotide antibiotic microcin C. Kulikovsky A, Serebryakova M, Bantysh O, Metlitskaya A, Borukhov S, Severinov K, Dubiley S.J Am Chem Soc. 2014 Aug 6;136(31):11168-75.
  2. The RimL transacetylase provides resistance to translation inhibitor microcin C. Kazakov T, Kuznedelov K, Semenova E, Mukhamedyarov D, Datsenko KA, Metlitskaya A, Vondenhoff GH, Tikhonov A, Agarwal V, Nair S, Van Aerschot A, Severinov K.J Bacteriol. 2014 Oct;196(19):3377-85
  3. High-throughput analysis of type I-E CRISPR/Cas spacer acquisition in E. coli.Savitskaya E, Semenova E, Dedkov V, Metlitskaya A, Severinov K.RNA Biol. 2013 May;10(5):716-25
  4. Structure and function of a serine carboxypeptidase adapted for degradation of the protein synthesis antibiotic microcin C7 .Agarwal V, Tikhonov A, Metlitskaya A, Severinov K, Nair SK.Proc Natl Acad Sci U S A. 2012 Mar 20;109(12):4425-30
  5. Structural basis for microcin C7 inactivation by the MccE acetyltransferase .Agarwal V, Metlitskaya A, Severinov K, Nair SK. J Biol Chem. 2011 Jun 17;286(24):21295-303.
  6. MccE provides resistance to protein synthesis inhibitor microcin C by acetylating the processed form of the antibiotic. Novikova M, Kazakov T, Vondenhoff GH, Semenova E, Rozenski J, Metlytskaya A, Zukher I, Tikhonov A, Van Aerschot A, Severinov K. J Biol Chem. 2010 Apr 23;285(17):12662-9
  7. Synthetic microcin C analogs targeting different aminoacyl-tRNA synthetases.Van de Vijver P, Vondenhoff GH, Kazakov TS, Semenova E, Kuznedelov K, Metlitskaya A, Van Aerschot A, Severinov K.J Bacteriol. 2009 Oct;191(20):6273-80. doi
  8. Maturation of the translation inhibitor microcin C.Metlitskaya A, Kazakov T, Vondenhoff GH, Novikova M, Shashkov A, Zatsepin T, Semenova E, Zaitseva N, Ramensky V, Van Aerschot A, Severinov K.J Bacteriol. 2009 Apr;191(7):2380-7
  9. Escherichia coli peptidase A, B, or N can process translation inhibitor microcin C. Kazakov T, Vondenhoff GH, Datsenko KA, Novikova M, Metlitskaya A, Wanner BL, Severinov K. J Bacteriol. 2008 Apr;190(7):2607-10
  10. The Escherichia coli Yej transporter is required for the uptake of translation inhibitor microcin C. Novikova M, Metlitskaya A, Datsenko K, Kazakov T, Kazakov A, Wanner B, Severinov K. J Bacteriol. 2007 Nov;189(22):8361-5
  11. Amino acid residues required for maturation, cell uptake, and processing of translation inhibitor microcin C. Kazakov T, Metlitskaya A, Severinov K. J Bacteriol. 2007 Mar;189(5):2114-8
  12. Aspartyl-tRNA synthetase is the target of peptide nucleotide antibiotic Microcin C. Metlitskaya A, Kazakov T, Kommer A, Pavlova O, Praetorius-Ibba M, Ibba M, Krasheninnikov I, Kolb V, Khmel I, Severinov K. J Biol Chem. 2006 Jun 30;281(26):18033-42.
  13. Production of N-acylhomoserine lactone signal molecules by gram-negative soil-borne and plant-associated bacteria. Veselova M, Kholmeckaya M, Klein S, Voronina E, Lipasova V, Metlitskaya A, Mayatskaya A, Lobanok E, Khmel I, Chernin L. Folia Microbiol (Praha). 2003;48(6):794-8.
  14. Microcin C51 plasmid genes: possible source of horizontal gene transfer. Fomenko DE, Metlitskaya AZ, Péduzzi J, Goulard C, Katrukha GS, Gening LV, Rebuffat S, Khmel IA. Antimicrob Agents Chemother. 2003 Sep;47(9):2868-74.
  15. Structure of microcin C51, a new antibiotic with a broad spectrum of activity. Metlitskaya AZ, Katrukha GS, Shashkov AS, Zaitsev DA, Egorov TA, Khmel IA. FEBS Lett. 1995 Jan 9;357(3):235-8.
  16. Cloning and mapping of the genetic determinants for microcin C51 production and immunity. Kurepina NE, Basyuk EI, Metlitskaya AZ, Zaitsev DA, Khmel IA. Mol Gen Genet. 1993 Dec;241(5-6):700-6.