Assembly, function and evolution of cyanobacterial carboxysomes

Kerfeld, Cheryl A.; Melnicki, Matthew R.

doi:10.1016/j.pbi.2016.03.009

Title: Assembly, function and evolution of cyanobacterial carboxysomes

Full Record
Other Related Research

Authors:: Kerfeld, Cheryl A.; Melnicki, Matthew R.

Publication Date:: 2016-06-01

Sponsoring Org.:: USDOE

OSTI Identifier:: 1357687

Grant/Contract Number:: FG02-91ER20021

Resource Type:: Publisher's Accepted Manuscript

Journal Name:: Current Opinion in Plant Biology

Additional Journal Information:: Journal Name: Current Opinion in Plant Biology Journal Volume: 31 Journal Issue: C; Journal ID: ISSN 1369-5266

Publisher:: Elsevier

Country of Publication:: United Kingdom

Language:: English

Citation Formats


                    Kerfeld, Cheryl A., and Melnicki, Matthew R.. Assembly, function and evolution of cyanobacterial carboxysomes.  United Kingdom: N. p., 2016. 
Web.  doi:10.1016/j.pbi.2016.03.009.

Copy to clipboard


                    Kerfeld, Cheryl A., & Melnicki, Matthew R.. Assembly, function and evolution of cyanobacterial carboxysomes.  United Kingdom.  https://doi.org/10.1016/j.pbi.2016.03.009

Copy to clipboard


                    Kerfeld, Cheryl A., and Melnicki, Matthew R.. Wed .  
"Assembly, function and evolution of cyanobacterial carboxysomes".  United Kingdom.  https://doi.org/10.1016/j.pbi.2016.03.009.

Copy to clipboard


                    
@article{osti_1357687,

  title        = {Assembly, function and evolution of cyanobacterial carboxysomes},

  author       = {Kerfeld, Cheryl A. and Melnicki, Matthew R.},

  abstractNote = {},

  doi          = {10.1016/j.pbi.2016.03.009},

  journal      = {Current Opinion in Plant Biology},

  number       = C,

  volume       = 31,

  place        = {United Kingdom},

  year         = {2016},

  month        = {6}

}

Copy to clipboard

Journal Article:

Free Publicly Available Full Text

Accepted Manuscript (Publisher)

Publisher's Version of Record
https://doi.org/10.1016/j.pbi.2016.03.009

Other availability

Search WorldCat to find libraries that may hold this journal

Citation Metrics:

Cited by: 127 works

Citation information provided by
Web of Science

Save / Share:

Export Metadata

Save to My Library

Similar Records in DOE PAGES and OSTI.GOV collections:

Cyanobacterial carboxysomes contain an unique rubisco-activase-like protein

Journal Article Lechno‐Yossef, Sigal ; Rohnke, Brandon A. ; Belza, Ana O. ; ... - New Phytologist

In plants, rubisco activase (Rca) regulates rubisco by removing inhibitory molecules such as ribulose–1,5–bisphosphate (RuBP). In cyanobacteria, a homologous protein (activase–like cyanobacterial protein, ALC), contains a distinctive C–terminal fusion resembling the small–subunit of rubisco. Although cyanobacterial rubisco is believed to be less sensitive to RuBP inhibition, the ALC is widely distributed among diverse cyanobacteria. Using microscopy, biochemistry and molecular biology, the cellular localization of the ALC, its effect on carboxysome/cell ultrastructure in Fremyella diplosiphon, and its function in vitro were studied. Bioinformatic analysis uncovered evolutionary relationships between the ALC and rubisco. ALC localizes to carboxysomes and exhibits ATPase activity. Furthermore,more »« less
Cited by 19
https://doi.org/10.1111/nph.16195

Full Text Available
Structure, function and evolution of the cyanobacterial orange carotenoid protein and its homologs

Journal Article Kerfeld, Cheryl A. ; Melnicki, Matthew R. ; Sutter, Markus ; ... - New Phytologist

Contents Summary 937 I. Introduction 937 II. The structure of the OCP 938 III. OCP function 939 IV. Distribution of OCPs, FRP and domains in cyanobacteria 943 V. Carotenoid–protein interactions in the OCP and the HCPs 947 VI. Conclusions and prospects 948 Acknowledgements 948 References 949 Summary The orange carotenoid protein ( OCP ) is a water‐soluble, photoactive protein involved in thermal dissipation of excess energy absorbed by the light‐harvesting phycobilisomes ( PBS ) in cyanobacteria. The OCP is structurally and functionally modular, consisting of a sensor domain, an effector domain and a keto‐carotenoid. On photoactivation, the OCP converts frommore »« less
Cited by 62
https://doi.org/10.1111/nph.14670

Full Text Available
Synthetic OCP heterodimers are photoactive and recapitulate the fusion of two primitive carotenoproteins in the evolution of cyanobacterial photoprotection

Journal Article Lechno‐Yossef, Sigal ; Melnicki, Matthew R. ; Bao, Han ; ... - The Plant Journal

Summary The orange carotenoid protein ( OCP ) governs photoprotection in the majority of cyanobacteria. It is structurally and functionally modular, comprised of a C‐terminal regulatory domain ( CTD ), an N‐terminal effector domain ( NTD ) and a ketocarotenoid; the chromophore spans the two domains in the ground state and translocates fully into the NTD upon illumination. Using both the canonical OCP 1 from Fremyella diplosiphon and the presumably more primitive OCP 2 paralog from the same organism, we show that an NTD ‐ CTD heterodimer forms when the domains are expressed as separate polypeptides. The carotenoid is requiredmore »« less
Cited by 24
https://doi.org/10.1111/tpj.13593

Full Text Available
β-Carboxysome bioinformatics: identification and evolution of new bacterial microcompartment protein gene classes and core locus constraints

Journal Article Sommer, Manuel ; Cai, Fei ; Melnicki, Matthew ; ... - Journal of Experimental Botany

Carboxysomes are bacterial microcompartments (BMCs) that enhance CO₂ fixation in all cyanobacteria. Structurally, carboxysome shell proteins are classified according to the type of oligomer formed: hexameric (BMC-H), trimeric (BMC-T) and pentameric (BMC-P) proteins. To understand the forces driving the evolution of the carboxysome shell, we conducted a bioinformatic study of genes encoding β-carboxysome shell proteins, taking advantage of the recent large increase in sequenced cyanobacterial genomes. In addition to the four well-established BMC-H (CcmK1-4) classes, our analysis reveals two new CcmK classes, which we name CcmK5 and CcmK6. CcmK5 is phylogenetically closest to CcmK3 and CcmK4, and the ccmK5 genemore »« less
Cited by 22
https://doi.org/10.1093/jxb/erx115

Full Text Available
RcaE-Dependent Regulation of Carboxysome Structural Proteins Has a Central Role in Environmental Determination of Carboxysome Morphology and Abundance in Fremyella diplosiphon

Journal Article Rohnke, Brandon A. ; Singh, Shailendra P. ; Pattanaik, Bagmi ; ... - mSphere

Carboxysomes are central to the carbon dioxide-concentrating mechanism (CCM) and carbon fixation in cyanobacteria. Although the structure is well understood, roles of environmental cues in the synthesis, positioning, and functional tuning of carboxysomes have not been systematically studied. Fremyella diplosiphon is a model cyanobacterium for assessing impacts of environmental light cues on photosynthetic pigmentation and tuning of photosynthetic efficiency during complementary chromatic acclimation (CCA), which is controlled by the photoreceptor RcaE. Given the central role of carboxysomes in photosynthesis, we investigated roles of light-dependent RcaE signaling in carboxysome structure and function. A ΔrcaE mutant exhibits altered carboxysome size and number,more »« less
Cited by 10
https://doi.org/10.1128/mSphere.00617-17

Similar Records