Different binding specificities of S-layer homology modules from Clostridium thermocellum AncA, Slp1, and Slp2.
S-layer homology (SLH) module polypeptides were derived from Clostridium thermocellum S-layer proteins Slp1 and Slp2 and cellulosome anchoring protein AncA as rSlp1-SLH, rSlp2-SLH, and rAncA-SLH respectively. Their binding specificities were investigated using C. thermocellum cell-wall preparations. rAncA-SLH associated with native peptidoglycan-containing sacculi from C. thermocellum, including both peptidoglycan and secondary cell wall polymers (SCWP), but not to hydrofluoric acid-extracted peptidoglycan-containing sacculi (HF-EPCS) lacking SCWPs, suggesting that SCWPs are responsible for binding with SLH modules of AncA. On the other hand, rSlp1-SLH and rSlp2-SLH associated with HF-EPCS, suggesting that these polypeptides had an affinity for peptidoglycan. A binding assay using a peptidoglycan fraction prepared from Escherichia coli cells definitely confirmed that rSlp1-SLH and rSlp2-SLH specifically interacted with peptidoglycan but not with SCWP.
Zhao
Guangshan
G
Faculty of Bioresources, Mie University, Tsu 514-8507, Japan.
Li
Huazhong
H
Wamalwa
Benson
B
Sakka
Makiko
M
Kimura
Tetsuya
T
Sakka
Kazuo
K
D000595:Amino Acid Sequence; D001426:Bacterial Proteins / Q000737:chemistry*; D002473:Cell Wall / Q000737:chemistry; D048013:Acetivibrio thermocellus / Q000737:chemistry*; D004926:Escherichia coli / Q000737:chemistry / Q000378:metabolism; D008565:Membrane Proteins / Q000737:chemistry*; D008969:Molecular Sequence Data; D010457:Peptidoglycan / Q000737:chemistry; D011485:Protein Binding; D017434:Protein Structure, Tertiary; D011993:Recombinant Fusion Proteins / Q000737:chemistry; D017386:Sequence Homology, Amino Acid
D001426:Bacterial Proteins; D008565:Membrane Proteins; D010457:Peptidoglycan; D011993:Recombinant Fusion Proteins