Abstract
The gene encoding the crystalline surface layer (S-layer) protein from Campylobacter rectus, designated slp, was sequenced and the recombinant gene product was expressed in Escherichia coli. The gene consisted of 4086 nucleotides encoding a protein with 1361 amino acids. The N-terminal amino acid sequence revealed that Slp did not contain a signal sequence, but that the initial methionine residue was processed. The deduced amino acid sequence displayed some common characteristic features of S-layer proteins previously reported. A homology search showed a high similarity to the Campylobacter fetus S-layer proteins, especially in their N-terminus. The C-terminal third of Slp exhibited homology with the RTX toxins from Gram-negative bacteria via the region including the glycine-rich repeats. The Slp protein had the same N-terminal sequence as a 104-kDa cytotoxin isolated from the culture supernatants of C. rectus. However, neither native nor recombinant Slp showed cytotoxicity against HL-60 cells or human peripheral white blood cells. These data support the idea that the N-terminus acts as an anchor to the cell surface components and that the C-terminus is involved in the assembly and/or transport of the protein.
| Original language | English |
|---|---|
| Pages (from-to) | 275-281 |
| Number of pages | 7 |
| Journal | FEMS Microbiology Letters |
| Volume | 166 |
| Issue number | 2 |
| Publication status | Published - Sep 15 1998 |
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Keywords
- Campylobacter rectus
- DNA sequencing
- RTX toxin
- S-layer
ASJC Scopus subject areas
- Genetics
- Molecular Biology
- Applied Microbiology and Biotechnology
- Microbiology
Cite this
The S-layer protein from Campylobacter rectus : Sequence determination and function of the recombinant protein. / Miyamoto, Manabu; Maeda, Hiroshi; Kitanaka, Michitaka; Kokeguchi, Susumu; Takashiba, Shogo; Murayama, Yoji.
In: FEMS Microbiology Letters, Vol. 166, No. 2, 15.09.1998, p. 275-281.Research output: Contribution to journal › Article
}
TY - JOUR
T1 - The S-layer protein from Campylobacter rectus
T2 - Sequence determination and function of the recombinant protein
AU - Miyamoto, Manabu
AU - Maeda, Hiroshi
AU - Kitanaka, Michitaka
AU - Kokeguchi, Susumu
AU - Takashiba, Shogo
AU - Murayama, Yoji
PY - 1998/9/15
Y1 - 1998/9/15
N2 - The gene encoding the crystalline surface layer (S-layer) protein from Campylobacter rectus, designated slp, was sequenced and the recombinant gene product was expressed in Escherichia coli. The gene consisted of 4086 nucleotides encoding a protein with 1361 amino acids. The N-terminal amino acid sequence revealed that Slp did not contain a signal sequence, but that the initial methionine residue was processed. The deduced amino acid sequence displayed some common characteristic features of S-layer proteins previously reported. A homology search showed a high similarity to the Campylobacter fetus S-layer proteins, especially in their N-terminus. The C-terminal third of Slp exhibited homology with the RTX toxins from Gram-negative bacteria via the region including the glycine-rich repeats. The Slp protein had the same N-terminal sequence as a 104-kDa cytotoxin isolated from the culture supernatants of C. rectus. However, neither native nor recombinant Slp showed cytotoxicity against HL-60 cells or human peripheral white blood cells. These data support the idea that the N-terminus acts as an anchor to the cell surface components and that the C-terminus is involved in the assembly and/or transport of the protein.
AB - The gene encoding the crystalline surface layer (S-layer) protein from Campylobacter rectus, designated slp, was sequenced and the recombinant gene product was expressed in Escherichia coli. The gene consisted of 4086 nucleotides encoding a protein with 1361 amino acids. The N-terminal amino acid sequence revealed that Slp did not contain a signal sequence, but that the initial methionine residue was processed. The deduced amino acid sequence displayed some common characteristic features of S-layer proteins previously reported. A homology search showed a high similarity to the Campylobacter fetus S-layer proteins, especially in their N-terminus. The C-terminal third of Slp exhibited homology with the RTX toxins from Gram-negative bacteria via the region including the glycine-rich repeats. The Slp protein had the same N-terminal sequence as a 104-kDa cytotoxin isolated from the culture supernatants of C. rectus. However, neither native nor recombinant Slp showed cytotoxicity against HL-60 cells or human peripheral white blood cells. These data support the idea that the N-terminus acts as an anchor to the cell surface components and that the C-terminus is involved in the assembly and/or transport of the protein.
KW - Campylobacter rectus
KW - DNA sequencing
KW - RTX toxin
KW - S-layer
UR - http://www.scopus.com/inward/record.url?scp=0032529965&partnerID=8YFLogxK
UR - http://www.scopus.com/inward/citedby.url?scp=0032529965&partnerID=8YFLogxK
M3 - Article
C2 - 9770285
AN - SCOPUS:0032529965
VL - 166
SP - 275
EP - 281
JO - FEMS Microbiology Letters
JF - FEMS Microbiology Letters
SN - 0378-1097
IS - 2
ER -