Characterization of Regulatory Elements of L11 and L1 Operons in Thermophilic Bacteria and Archaea

Biochemistry (Mosc). 2021 Apr;86(4):397-408. doi: 10.1134/S0006297921040027.


Ribosomal protein L1 is a conserved two-domain protein that is involved in formation of the L1 stalk of the large ribosomal subunit. When there are no free binding sites available on the ribosomal 23S RNA, the protein binds to the specific site on the mRNA of its own operon (L11 operon in bacteria and L1 operon in archaea) preventing translation. Here we show that the regulatory properties of the r-protein L1 and its domain I are conserved in the thermophilic bacteria Thermus and Thermotoga and in the halophilic archaeon Haloarcula marismortui. At the same time the revealed features of the operon regulation in thermophilic bacteria suggest presence of two regulatory regions.

Keywords: L1 operon; L11 operon; mRNA; r-proteins; regulation of expression.

MeSH terms

  • Gene Expression Regulation, Archaeal
  • Gene Expression Regulation, Bacterial
  • Haloarcula marismortui / genetics*
  • Haloarcula marismortui / metabolism
  • Hot Temperature
  • Operon / genetics*
  • Regulatory Sequences, Nucleic Acid*
  • Ribosomal Proteins / genetics*
  • Thermotoga maritima / genetics*
  • Thermotoga maritima / metabolism
  • Thermus thermophilus / genetics*
  • Thermus thermophilus / metabolism


  • Ribosomal Proteins
  • ribosomal protein L1
  • ribosomal protein L11