Genetic engineering and overexpression of ribosomal L12 protein genes from three different archaebacteria in E coli.

  title={Genetic engineering and overexpression of ribosomal L12 protein genes from three different archaebacteria in E coli.},
  author={A K K{\"o}pke and Frank Hannemann and Tobias Boeckh},
  volume={73 6},
1 Citations


Complete nucleotide sequence of the ribosomal 'A' protein operon from the archaebacterium, Halobacterium halobium.
  • T. Itoh
  • Biology
    European journal of biochemistry
  • 1988
DNA fragments cloned from the halophilic archaebacterium Halobacterium halobium including the gene for ribosomal 'A' protein (HhaL20) were sequenced. Sequence and transcript analyzes indicated that
Comparative studies of ribosomal proteins and their genes from Methanococcus vannielii and other organisms.
Using data from a partial protein sequence analysis of ribosomal proteins derived from the archaebacterium Methanococcus vannielii, oligonucleotide probes were synthesized and amino acid sequences were deduced that were more related to the eukaryotic kingdom than to the Gram-positive or Gram-negative eubacteria.
Structure and evolution of the L11, L1, L10, and L12 equivalent ribosomal proteins in eubacteria, archaebacteria, and eucaryotes.
Alignment of the proline-rich L11e proteins reveals that the N-terminal region, believed to be responsible for interaction with release factor 1, is the most highly conserved region and that there is specific conservation of most of theProline residues, which may be important in maintaining the highly elongated structure of the molecule.
Occurrence in the archaebacterium Sulfolobus solfataricus of a ribosomal protein complex corresponding to Escherichia coli (L7/L12)4.L10 and eukaryotic (P1)2/(P2)2.P0.
The occurrence in an archaebacterium of a complex of acidic ribosomal proteins similar to E. coli (L7/L12)4 strongly supports the concept that this element of quaternary structure is a major conserved feature of the ribosome and reaffirms its importance in the translocation step of protein synthesis.
Ribosomal protein interactions in yeast
The results indicate that protein L15 might be equivalent to bacterial ribosomal protein L10 in forming a complex with the acidic proteins, and suggest strongly thatprotein L15 plays the same role in the yeast ribosome as proteins L10 and L11 do in the bacterial particles.