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Structural insight into the cooperation of chloroplast chaperonin subunits

Overview of attention for article published in BMC Biology, April 2016
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Title
Structural insight into the cooperation of chloroplast chaperonin subunits
Published in
BMC Biology, April 2016
DOI 10.1186/s12915-016-0251-8
Pubmed ID
Authors

Shijia Zhang, Huan Zhou, Feng Yu, Cuicui Bai, Qian Zhao, Jianhua He, Cuimin Liu

Abstract

Chloroplast chaperonin, consisting of multiple subunits, mediates folding of the highly abundant protein Rubisco with the assistance of co-chaperonins. ATP hydrolysis drives the chaperonin allosteric cycle to assist substrate folding and promotes disassembly of chloroplast chaperonin. The ways in which the subunits cooperate during this cycle remain unclear. Here, we report the first crystal structure of Chlamydomonas chloroplast chaperonin homo-oligomer (CPN60β1) at 3.8 Å, which shares structural topology with typical type I chaperonins but with looser compaction, and possesses a larger central cavity, less contact sites and an enlarged ATP binding pocket compared to GroEL. The overall structure of Cpn60 resembles the GroEL allosteric intermediate state. Moreover, two amino acid (aa) residues (G153, G154) conserved among Cpn60s are involved in ATPase activity regulated by co-chaperonins. Domain swapping analysis revealed that the monomeric state of CPN60α is controlled by its equatorial domain. Furthermore, the C-terminal segment (aa 484-547) of CPN60β influenced oligomer disassembly and allosteric rearrangement driven by ATP hydrolysis. The entire equatorial domain and at least one part of the intermediate domain from CPN60α are indispensable for functional cooperation with CPN60β1, and this functional cooperation is strictly dependent on a conserved aa residue (E461) in the CPN60α subunit. The first crystal structure of Chlamydomonas chloroplast chaperonin homo-oligomer (CPN60β1) is reported. The equatorial domain maintained the monomeric state of CPN60α and the C-terminus of CPN60β affected oligomer disassembly driven by ATP. The cooperative roles of CPN60 subunits were also established.

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Mendeley readers

The data shown below were compiled from readership statistics for 28 Mendeley readers of this research output. Click here to see the associated Mendeley record.

Geographical breakdown

Country Count As %
Chile 1 4%
Unknown 27 96%

Demographic breakdown

Readers by professional status Count As %
Researcher 7 25%
Student > Master 5 18%
Student > Ph. D. Student 5 18%
Student > Doctoral Student 3 11%
Student > Bachelor 3 11%
Other 2 7%
Unknown 3 11%
Readers by discipline Count As %
Biochemistry, Genetics and Molecular Biology 13 46%
Agricultural and Biological Sciences 8 29%
Pharmacology, Toxicology and Pharmaceutical Science 1 4%
Physics and Astronomy 1 4%
Medicine and Dentistry 1 4%
Other 1 4%
Unknown 3 11%

Attention Score in Context

This research output has an Altmetric Attention Score of 1. This is our high-level measure of the quality and quantity of online attention that it has received. This Attention Score, as well as the ranking and number of research outputs shown below, was calculated when the research output was last mentioned on 14 June 2016.
All research outputs
#5,707,353
of 7,896,890 outputs
Outputs from BMC Biology
#766
of 852 outputs
Outputs of similar age
#171,991
of 267,985 outputs
Outputs of similar age from BMC Biology
#22
of 25 outputs
Altmetric has tracked 7,896,890 research outputs across all sources so far. This one is in the 24th percentile – i.e., 24% of other outputs scored the same or lower than it.
So far Altmetric has tracked 852 research outputs from this source. They typically receive a lot more attention than average, with a mean Attention Score of 14.3. This one is in the 7th percentile – i.e., 7% of its peers scored the same or lower than it.
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We're also able to compare this research output to 25 others from the same source and published within six weeks on either side of this one. This one is in the 4th percentile – i.e., 4% of its contemporaries scored the same or lower than it.