RRC ID |
57312
|
Author |
Goda S, Koga T, Yamashita K, Kuriura R, Ueda T.
|
Title |
A novel carbohydrate-binding surface layer protein from the hyperthermophilic archaeon Pyrococcus horikoshii.
|
Journal |
Biosci Biotechnol Biochem
|
Abstract |
In Archaea and Bacteria, surface layer (S-layer) proteins form the cell envelope and are involved in cell protection. In the present study, a putative S-layer protein was purified from the crude extract of Pyrococcus horikoshii using affinity chromatography. The S-layer gene was cloned and expressed in Escherichia coli. Isothermal titration calorimetry analyses showed that the S-layer protein bound N-acetylglucosamine and induced agglutination of the gram-positive bacterium Micrococcus lysodeikticus. The protein comprised a 21-mer structure, with a molecular mass of 1,340 kDa, as determined using small-angle X-ray scattering. This protein showed high thermal stability, with a midpoint of thermal denaturation of 79 °C in dynamic light scattering experiments. This is the first description of the carbohydrate-binding archaeal S-layer protein and its characteristics.
|
Volume |
82(8)
|
Pages |
1327-1334
|
Published |
2018-8-1
|
DOI |
10.1080/09168451.2018.1460571
|
PMID |
29629656
|
MeSH |
Acetylglucosamine / metabolism*
Amino Acid Sequence
Archaeal Proteins / chemistry
Archaeal Proteins / genetics
Archaeal Proteins / isolation & purification
Archaeal Proteins / metabolism*
Calorimetry / methods
Chromatography, Affinity / methods
Cloning, Molecular
Electrophoresis, Polyacrylamide Gel
Escherichia coli / genetics
Genes, Archaeal
Green Fluorescent Proteins / metabolism
Hot Temperature
Micrococcus / metabolism
Protein Binding
Protein Conformation
Protein Denaturation
Protein Stability
Pyrococcus horikoshii / metabolism*
Scattering, Small Angle
X-Ray Diffraction
|
IF |
1.297
|
Times Cited |
0
|
Resource |
General Microbes |
JCM 9975 |