Figure - PMC

Skip to main content

An official website of the United States government

Here's how you know

Here's how you know

Official websites use .gov
A .gov website belongs to an official government organization in the United States.

Secure .gov websites use HTTPS
A lock ( ) or https:// means you've safely connected to the .gov website. Share sensitive information only on official, secure websites.

View full-text article in PMC

. 2011 Apr 5;9(4):e1001040. doi: 10.1371/journal.pbio.1001040

Search in PMC
Search in PubMed
View in NLM Catalog
Add to search

Peng et al.

This is an open-access article distributed under the terms of the Creative Commons Attribution License, which permits unrestricted use, distribution, and reproduction in any medium, provided the original author and source are properly credited.

PMC Copyright notice

(A) Cpn60β4 is localized to the chloroplast stroma. Freshly isolated chloroplasts from various genotypes were separated into membrane and stromal fractions. Immunoblot analysis was performed using the indicated antibodies. RbcL and Cyt f were detected as loading and fractionation controls. (B) Stromal protein complexes isolated from crr27-1 complemented by Cpn60β4-HA were separated by CN-PAGE, followed by 2-dimensional SDS-PAGE. The proteins were immunodetected with specific antibodies. A short arrow indicates the position of the Cpn60 complex. (C) Heterooligomeric complex formation between Cpn60β4, Cpn60α1, and Cpn60β1–β3. Chaperonin complex containing Cpn60β4 was purified from the crr27-1 mutant plants expressing HA-tagged Cpn60β4 using the µMACS HA isolation kit. After elution, total proteins were separated by 7.5% SDS-PAGE and stained with CBB. The signals were quantitatively analyzed with Imagemaster software (Amersham Pharmacia Biotech). The stoichiometry of Cpn60β4, Cpn60β1–β3, and Cpn60α1 in the specific chaperonin complex containing Cpn60β4 was estimated to be 17:37:46 and 14:39:47 in the two independent purifications (E1 and E2), respectively.