Elsevier

FEBS Letters

Volume 340, Issues 1–2, 28 February 1994, Pages 25-28
FEBS Letters

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

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Abstract

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.

Keywords

cDNA cloning
Lon protease
ATP-dependent proteolysis
Long 5'-untranslated region
Human mRNA

Abbreviations

LonBB, B. brevis Lon protease
LonEC,E. coli Lon protease
LonHS,H. sapiens putative Lon protease
LonMX,M. xanthus Lon protease
ORF, open reading frame
UTR, untranslated region
NTP, nucleoside triphosphate.

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