Open AccessSynthesis of a small, cysteine‐rich, 29 amino acids long peptide in Mycoplasma pneumoniae
Author(s) -
Zimmerman C.U.,
Herrmann R.
Publication year - 2005
Publication title -
fems microbiology letters
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 0.899
H-Index - 151
eISSN - 1574-6968
pISSN - 0378-1097
DOI - 10.1016/j.femsle.2005.09.054
Subject(s) - open reading frame , mycoplasma pneumoniae , edman degradation , peptide , amino acid , peptide sequence , biology , gene , cysteine , molecular mass , fusion protein , microbiology and biotechnology , biochemistry , chemistry , recombinant dna , medicine , enzyme , pneumonia
A 205–210 bases long, small RNA (MP200RNA) of Mycoplasma pneumoniae encodes an open reading frame (ORF pmp200 ) that has the potential to be translated into a 29 amino acids long peptide with nine cysteines. The expression of this peptide in M. pneumoniae was proven indirectly by constructing a gene fusion between the ORF pmp200 and mrfp1 , the gene encoding the monomeric red fluorescent protein. The fusion construct was translated in M. pneumoniae . The corresponding fusion protein, with a molecular mass of approximately 35,000 Da, was isolated and the correct sequence was proven by Edman degradation and by mass spectrometry