Purification, crystallization and preliminary X-ray diffraction analysis of the Hsp40 protein CPIP1 from Nicotiana tabacum.
Chaperones promote many different molecular processes, including the folding, targeting and degradation of proteins. The best-studied chaperone system consists of the Hsp70s and their co-chaperones the Hsp40s. Chaperone function can be hijacked by viruses in plants. Potato virus Y interacts via its coat protein with an Hsp40 from Nicotiana tabacum, referred to as NtCPIP1, in order to regulate replication. To understand the molecular determinants of this mechanism, different variants of NtCPIP1 were expressed, purified and crystallized. While crystals of wild-type NtCPIP1 diffracted to 8.0 Å resolution, the deletion mutant NtCPIP1-Δ(1:127) crystallized in space group P2(1)2(1)2 and diffracted to 2.4 Å resolution.
Lehrstuhl für Biotechnik, Department of Biology, Friedrich-Alexander University Erlangen-Nuremberg, Erlangen, Germany.
Martin H
MH
Griessl
Isabel
I
Jungkunz
Uwe
U
Sonnewald
Yves A
YA
Muller
D003460:Crystallization; D018360:Crystallography, X-Ray; D050956:HSP40 Heat-Shock Proteins / Q000737:chemistry* / Q000302:isolation & purification; D010940:Plant Proteins / Q000737:chemistry* / Q000302:isolation & purification; D014026:Nicotiana
D050956:HSP40 Heat-Shock Proteins; D010940:Plant Proteins