Mapping the interaction site of prion protein and Sho.
The cellular prion protein (PrP(C)) is a highly conserved protein among mammals and is considered to have important cellular functions. Despite decades of intensive research, however, the physiological function of PrP(C) remains unclear. Sho (Shadoo, shadow of prion protein) and PrP(C) have similar N-terminals, which suggests that the two proteins share biological functions. Using truncation mutants of both proteins and yeast two-hybrid analysis, with validation by co-immunoprecipitation and surface plasmon resonance (SPR), we have identified an interaction between Sho 61-77 and PrP(C) 108-126 domains. This indicates that Sho may play a role in the physiological function of PrP(C) and prion pathogenesis.
Jiayu
Wan
W
Institute of Military Veterinary, Academy of Military Medical Sciences, 1068 Qinglong Road, Changchun, 130062 China.
Zhu
Hao
H
Ming
Xu
X
Xiong
Wang
W
Songbo
Wu
W
Bocui
Song
S
Wensen
Liu
L
Jiping
Li
L
Keying
Meng
M
Zhongyi
Li
L
Hongwei
Gao
G
D000818:Animals; D058851:GPI-Linked Proteins; D047468:Immunoprecipitation; D051379:Mice; D009419:Nerve Tissue Proteins / Q000737:chemistry / Q000378:metabolism*; D011328:Prions / Q000737:chemistry / Q000378:metabolism*; D011485:Protein Binding; D025941:Protein Interaction Mapping; D017434:Protein Structure, Tertiary; D015203:Reproducibility of Results; D020349:Surface Plasmon Resonance; D020798:Two-Hybrid System Techniques
D058851:GPI-Linked Proteins; D009419:Nerve Tissue Proteins; D011328:Prions; C523856:Sprn protein, mouse
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