Structure and evolution of the repetitive gene encoding streptococcal protein G.
The complete sequence of the structural gene encoding the immunoglobulin G binding protein from Streptococcus G148 has been determined, as well as its 5' and 3' flanking sequences. The sequence reveals an open reading frame encoding a putative preprotein with a relative molecular mass of 63294. N-Terminal sequencing of the mature protein, spontaneously released from streptococcal cells, demonstrates that the signal peptide consists of 33 amino acids. The DNA sequence reveals extensive internal homologies similar to other cell-wall-bound receptors from gram-positive bacteria. Comparisons with a related gene previously isolated from another strain of streptococci revealed large differences in size, due to variations in the number of internal repeats. The structure of the gene suggests an evolution through multiple duplications.
Olsson
A
A
Department of Biochemistry, Royal Institute of Technology, Stockholm, Sweden.
Eliasson
M
M
Guss
B
B
Nilsson
B
B
Hellman
U
U
Lindberg
M
M
Uhlén
M
M
D000595:Amino Acid Sequence; D001426:Bacterial Proteins / Q000235:genetics* / Q000276:immunology; D001483:Base Sequence; D005075:Biological Evolution; D005796:Genes; D005803:Genes, Immunoglobulin; D005815:Genetic Code; D007133:Immunoglobulin Joining Region / Q000235:genetics*; D008969:Molecular Sequence Data; D021382:Protein Sorting Signals / Q000235:genetics; D012689:Sequence Homology, Nucleic Acid
D001426:Bacterial Proteins; C034284:IgG Fc-binding protein, Streptococcus; D007133:Immunoglobulin Joining Region; D021382:Protein Sorting Signals