Cloning and sequence analysis of cDNA for a human homolog of eubacterial ATP-dependent Lon proteases

FEBS Lett. 1994 Feb 28;340(1-2):25-8. doi: 10.1016/0014-5793(94)80166-5.


Overlapping cDNA clones containing mRNA for a putative Lon protease (LonHS) were isolated from cDNA libraries prepared from human brain poly(A)+ RNA. The determined nucleotide sequence contains a 2814-bp open reading frame with two potential initiation codons (positions 62-64 and 338-340). The 5'-terminal 337-nucleotide fragment of LonHS mRNA is highly enriched with G and C nucleotides and could direct synthesis of the LonHS N-terminal domain. More likely this region promotes initiation of protein synthesis from the second AUG codon in a cap-independent manner. The amino acid sequence initiated at the second AUG codon includes 845 residues, over 30% of which are identical to those of eubacterial Lon proteases. Residues of the 'A' and 'B' motifs of NTP-binding pattern and a plausible catalytic serine residue are conserved in LonHS. Northern blot analysis revealed LonHS mRNA in lung, duodenum, liver and heart, but not in thymus cells.

Publication types

  • Research Support, Non-U.S. Gov't

MeSH terms

  • ATP-Dependent Proteases
  • Amino Acid Sequence
  • Animals
  • Base Sequence
  • Brain / enzymology*
  • Cloning, Molecular
  • DNA, Complementary
  • Escherichia coli / enzymology
  • Escherichia coli Proteins*
  • Heat-Shock Proteins / genetics*
  • Humans
  • Molecular Sequence Data
  • Protease La*
  • Rats
  • Sequence Analysis, DNA
  • Sequence Homology, Amino Acid
  • Serine Endopeptidases / genetics*
  • Tissue Distribution


  • DNA, Complementary
  • Escherichia coli Proteins
  • Heat-Shock Proteins
  • ATP-Dependent Proteases
  • Serine Endopeptidases
  • Lon protein, E coli
  • Protease La

Associated data

  • GENBANK/X74215
  • GENBANK/X76040