Skip to content
DraconiticResearch
Search Sources API
201,683 studies31 sourcesUpdated 25 min ago
Peer-reviewedCC BY-NC-NDNano letters

Broad Stability and pH-Mediated Reversible Disassembly of In Vitro Assembled Bacterial Microcompartment Shells.

  • Kyleigh L Range1
  • Timothy K Chiang1
  • Antonino Caliò2
  • Arinita Pramanik1
  • Greg L Hura2,3
  • Markus Sutter2,4,5
  • Cheryl A Kerfeld2,4,5,6
6 affiliations
  1. 1Molecular Foundry Division, Lawrence Berkeley National Laboratory, Berkeley, California94720, United States.
  2. 2Molecular Biophysics and Integrated Bioimaging Division, Lawrence Berkeley National Laboratory, Berkeley, California94720, United States.
  3. 3Department of Chemistry and Biochemistry, University of California, Santa Cruz, California95064, United States.
  4. 4MSU-DOE Plant Research Laboratory, Michigan State University, East Lansing, Michigan48824, United States.
  5. 5Environmental Genomics and Systems Biology Division, Lawrence Berkeley National Laboratory, Berkeley, California94720, United States.
  6. 6Department of Biochemistry and Molecular Biology, Michigan State University, East Lansing, Michigan48824, United States.
Read full textPDFDOICite

Abstract

Bacterial microcompartments (BMCs) are self-assembling organelles that colocalize enzymes and metabolites of various biochemical pathways. Their selectively permeable shell is made entirely of protein, and the inherent properties of these systems make them attractive templates for bioengineering synthetic nanoreactors. Understanding the extent of shell stability in an extended range of conditions broadens the scope of chemistries that can be confined in these nanocompartments. Here we analyze the stability of in vitro assembled BMC shells and find that they retain their structure at high concentrations of various solvents and detergents, at temperatures up to 75 °C, and across a pH range from 3.9 to 11. Shell disassembly is observed below pH 3.9, but shells can be reassembled upon increasing the pH back to 8. These results expand the range of reactions that can be performed inside protein-based nanoreactors and underscore the potential of modular BMC shell proteins as versatile biomaterials.

Related

  1. A bacterial Rhesus transporter retunes a structurally conserved ammonium pore into a reversible nitrogen valve
    A. Bizior, M. Qin, P. Henderson +7
    bioRxivPreprintCC BYFull textEnzymology & metabolismbioRxiv
  2. BOULE is Essential for the Dynamic Disassembly of Heat Shock Granules in Male Germ Cells
    Xin Li, Nana Zhang, Zexin Bian +6
    Advanced SciencePeer-reviewedCC BY 4.0Full textMolecular biology & gene regulationPMC
  3. Polymer Polydispersity and Lipid Composition Control Nanoplastic Disassembly in Membranes
    H. Ghermezcheshme, K. Bisht, S. O. Yesylevskyy +1
    bioRxivPreprintCC BY-NDFull textBiophysicsbioRxiv
  4. A protein–foldamer supramolecular synthon for self-assembled hybrid architectures
    Johannes Sigl, Vasily Morozov, Lingfei Wang +14
    Nature Chemistry-Peer-reviewedPublisher termsFull text2 citedStructural biologyGeneral biologyHAL
  5. Self‐Assembled Monolayers on Gold Surfaces of Ferrocene‐BODIPY‐Fullerene‐Helical Peptide Conjugates: Studies of Electron Transfer Processes by Ultra‐Fast Electrochemistry
    Jad Rabah, Anne Vallée, Hélène Fensterbank +6
    Journal of Peptide SciencePeer-reviewedCC BY 4.0Full textMolecular biology & gene regulationPMC

Cite

BibTeXRIS
BibTeX
@article{range2026broad,
  title = {{Broad Stability and pH-Mediated Reversible Disassembly of In Vitro Assembled Bacterial Microcompartment Shells.}},
  author = {Kyleigh L Range and Timothy K Chiang and Antonino Caliò and Arinita Pramanik and Greg L Hura and Markus Sutter and Cheryl A Kerfeld},
  journal = {Nano letters},
  year = {2026},
  month = oct,
  doi = {10.1021/acs.nanolett.6c02629},
  url = {https://europepmc.org/article/MED/42905059},
  note = {CC BY-NC-ND},
}
RIS
TY  - JOUR
TI  - Broad Stability and pH-Mediated Reversible Disassembly of In Vitro Assembled Bacterial Microcompartment Shells.
AU  - Kyleigh L Range
AU  - Timothy K Chiang
AU  - Antonino Caliò
AU  - Arinita Pramanik
AU  - Greg L Hura
AU  - Markus Sutter
AU  - Cheryl A Kerfeld
PY  - 2026
DA  - 2026/10/01
JO  - Nano letters
DO  - 10.1021/acs.nanolett.6c02629
UR  - https://europepmc.org/article/MED/42905059
AB  - Bacterial microcompartments (BMCs) are self-assembling organelles that colocalize enzymes and metabolites of various biochemical pathways. Their selectively permeable shell is made entirely of protein, and the inherent properties of these systems make them attractive templates for bioengineering synthetic nanoreactors. Understanding the extent of shell stability in an extended range of conditions broadens the scope of chemistries that can be confined in these nanocompartments. Here we analyze the stability of in vitro assembled BMC shells and find that they retain their structure at high concentrations of various solvents and detergents, at temperatures up to 75 °C, and across a pH range from 3.9 to 11. Shell disassembly is observed below pH 3.9, but shells can be reassembled upon increasing the pH back to 8. These results expand the range of reactions that can be performed inside protein-based nanoreactors and underscore the potential of modular BMC shell proteins as versatile biomaterials.
SN  - 1530-6984
SN  - 1530-6992
ER  -