Premium
Cloning and sequence analysis of cDNA for a human homolog of eubacterial ATP‐dependent Lon proteases
Author(s) -
Amerik Alexander Yu.,
Petukhova Galina V.,
Grigorenko Vitaly G.,
Lykov Igor P.,
Yarovoi Serge V.,
Lipkin Valery M.,
Gorbalenya Alexander E.
Publication year - 1994
Publication title -
febs letters
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.593
H-Index - 257
eISSN - 1873-3468
pISSN - 0014-5793
DOI - 10.1016/0014-5793(94)80166-5
Subject(s) - complementary dna , biology , microbiology and biotechnology , open reading frame , nucleic acid sequence , serine , peptide sequence , messenger rna , proteases , conserved sequence , serine protease , biochemistry , start codon , sequence analysis , gene , protease , enzyme
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.