
Molecular cloning and sequence analysis of the gene coding for the 57‐kDa major soluble antigen of the salmonid fish pathogen Renibacterium salmoninarum
Author(s) -
Chien MawSheng,
Gilbert Teresa L.,
Huang Chienjin,
Landolt Marsha L.,
O'Hara Patrick J.,
Winton James R.
Publication year - 1992
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 - 10.1111/j.1574-6968.1992.tb05427.x
Subject(s) - open reading frame , biology , peptide sequence , amino acid , gene , nucleic acid sequence , microbiology and biotechnology , coding region , biochemistry , sequence analysis , molecular cloning
The complete sequence coding for the 57‐kDa major soluble antigen of the salmonid fish pathogen, Renibacterium salmoninarum , was determined. The gene contained an opening reading frame of 1671 nucleotides coding for a protein of 557 amino acids with a calculated M r value of 57190. The first 26 amino acids constituted a signal peptide. The deduced sequence for amino acid residues 27–61 was in agreement with the 35 N‐terminal amino acid residues determined by microsequencing, suggesting the protein in synthesized as a 557‐amino acid precursor and processed to produce a mature protein of M r 54505. Two regions of the protein contained imperfect direct repeats. The first region contained two copies of an 81‐residue repeat, the second contained five copies of an unrelated 25‐residue repeat. Also, a perfect inverted repeat (including three in‐frame UAA stop codons) was observed at the carboxyl‐terminus of the gene.