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Purification, crystallization and preliminary X-ray diffraction analysis of the Hsp40 protein CPIP1 from Nicotiana tabacum.

ABSTRACT: 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-?(1:127) crystallized in space group P2(1)2(1)2 and diffracted to 2.4 Å resolution.

SUBMITTER: Griessl MH

PROVIDER: S-EPMC3274412 | biostudies-literature | 2012 Feb

REPOSITORIES: biostudies-literature

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Purification, crystallization and preliminary X-ray diffraction analysis of the Hsp40 protein CPIP1 from Nicotiana tabacum.

Griessl Martin H MH Jungkunz Isabel I Sonnewald Uwe U Muller Yves A YA

Acta crystallographica. Section F, Structural biology and crystallization communications 20120127 Pt 2

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 w ...[more]

PMID: 22298008

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