A Tunable Protein Piston That Breaks Membranes to Release Encapsulated Cargo

ACS Synthetic Biology

Volumn 5, Issue 4, 2016, Pages 303-311

  Polka, Jessica K ^a,b   Silver, Pamela A ^a,b  

^a HARVARD MEDICAL SCHOOL   (United States)

^b HARVARD UNIVERSITY   (United States)

Author keywords

bioengineering; biotechnology; conformational change; Kappa particles; protein assembly; refractile bodies

Indexed keywords

BACTERIAL PROTEIN; RECOMBINANT PROTEIN;

ARTICLE; BIOTECHNOLOGY; CELL COMPARTMENTALIZATION; CELL MEMBRANE; CIRCULAR DICHROISM; CONFORMATIONAL TRANSITION; ENDOSYMBIONT; ESCHERICHIA COLI; HIGH THROUGHPUT SCREENING; IONIC STRENGTH; NONHUMAN; NUCLEAR REPROGRAMMING; PARAMECIUM; PH; PRIORITY JOURNAL; PROTEIN ASSEMBLY; PROTEIN SECONDARY STRUCTURE; SYNTHETIC BIOLOGY; AMINO ACID SEQUENCE; BIOSYNTHESIS; CELL INCLUSION; CELL WALL; CHEMISTRY; ELECTRON MICROSCOPY; GENE VECTOR; GENETICS; ISOLATION AND PURIFICATION; METABOLISM; MOLECULAR GENETICS; OSMOLARITY; SEQUENCE ALIGNMENT; SITE DIRECTED MUTAGENESIS; SPECTROPHOTOMETRY;

AMINO ACID SEQUENCE; BACTERIAL PROTEINS; CELL WALL; CIRCULAR DICHROISM; ESCHERICHIA COLI; GENETIC VECTORS; HYDROGEN-ION CONCENTRATION; INCLUSION BODIES; MICROSCOPY, ELECTRON; MOLECULAR SEQUENCE DATA; MUTAGENESIS, SITE-DIRECTED; OSMOLAR CONCENTRATION; RECOMBINANT PROTEINS; SEQUENCE ALIGNMENT; SPECTROPHOTOMETRY;

EID: 84966270241     PISSN: None     EISSN: 21615063     Source Type: Journal    
DOI: 10.1021/acssynbio.5b00237     Document Type: Article

References (29)

1. Pond, F. R., Gibson, I., Lalucat, J., and Quackenbush, R. L. (1989) R-body-producing bacteria Microbiol. Rev. 53, 25-67
2. Mueller, J. A. (1965) Vitally stained kappa in Paramecium aurelia J. Exp. Zool. 160, 369-372 10.1002/jez.1401600314
3. Sonneborn, T. M., Jacobson, W., and Dippell, R. V. (1946) Paramecin 51, an antibiotic produced by Paramecium aurelia; amounts released from killers and taken up by sensitives; conditions protecting sensitives Anat. Rec. 96, 514
4. Austin, M. L. (1946) Contributions towards an analysis of the killing action of variety 4 killers in Paramecium aurelia Anat. Rec. 96, 514
5. Jurand, A., Rudman, B. M., and Preer, J. R. (1971) Prelethal effects of killing action by stock 7 of Paramecium aurelia J. Exp. Zool. 177, 365-387 10.1002/jez.1401770311
6. Preer, L. B., Jurand, A., Preer, J. R., and Rudman, B. M. (1972) The Classes of Kappa in Paramecium Aurelia J. Cell Sci. 11, 581-600
7. Quackenbush, R. L. and Burbach, J. A. (1983) Cloning and expression of DNA sequences associated with the killer trait of Paramecium tetraurelia stock 47 Proc. Natl. Acad. Sci. U. S. A. 80, 250-254 10.1073/pnas.80.1.250
8. Schrallhammer, M., Galati, S., Altenbuchner, J., Schweikert, M., Görtz, H.-D., and Petroni, G. (2012) Tracing the role of R-bodies in the killer trait: Absence of toxicity of R-body producing recombinant E. coli on paramecia Eur. J. Protistol. 48, 290-296 10.1016/j.ejop.2012.01.008
9. Preer, J. R., Jr., Hufnagel, L. A., and Preer, L. B. (1966) Structure and behavior of R bodies from killer paramecia J. Ultrastruct. Res. 15, 131-143 10.1016/S0022-5320(66)80100-4
10. Kanabrocki, J. A., Quackenbush, R. L., and Pond, F. R. (1986) Organization and expression of genetic determinants for synthesis and assembly of type 51 R bodies J. Bacteriol. 168, 40-48
11. Heruth, D. P., Pond, F. R., Dilts, J. A., and Quackenbush, R. L. (1994) Characterization of genetic determinants for R body synthesis and assembly in Caedibacter taeniospiralis 47 and 116 J. Bacteriol. 176, 3559-3567
12. Jeblick, J. and Kusch, J. (2005) Sequence, Transcription Activity, and Evolutionary Origin of the R-BodyCoding Plasmid pKAP298 from the Intracellular Parasitic BacteriumCaedibacter taeniospiralis J. Mol. Evol. 60, 164-173 10.1007/s00239-004-0002-2
13. Pace, C. N. and Scholtz, J. M. (1998) A helix propensity scale based on experimental studies of peptides and proteins Biophys. J. 75, 422-427 10.1016/S0006-3495(98)77529-0
14. Martinez, K. A., Kitko, R. D., Mershon, J. P., Adcox, H. E., Malek, K. A., Berkmen, M. B., and Slonczewski, J. L. (2012) Cytoplasmic pH response to acid stress in individual cells of Escherichia coli and Bacillus subtilis observed by fluorescence ratio imaging microscopy Appl. Environ. Microbiol. 78, 3706-3714 10.1128/AEM.00354-12
15. Harrison, S. C. (2008) Viral membrane fusion Nat. Struct. Mol. Biol. 15, 690-698 10.1038/nsmb.1456
16. Canton, J., Khezri, R., Glogauer, M., and Grinstein, S. (2014) Contrasting phagosome pH regulation and maturation in human M1 and M2 macrophages Mol. Biol. Cell 25, 3330-3341 10.1091/mbc.E14-05-0967
17. Raymann, K., Bobay, L.-M., Doak, T. G., Lynch, M., and Gribaldo, S. (2013) A Genomic Survey of Reb Homologs Suggests Widespread Occurrence of R-Bodies in Proteobacteria G3: Genes, Genomes, Genet. 3, 505-516 10.1534/g3.112.005231
18. Shaner, N. C., Lambert, G. G., Chammas, A., Ni, Y., Cranfill, P. J., Baird, M. A., Sell, B. R., Allen, J. R., Day, R. N., Israelsson, M., Davidson, M. W., and Wang, J. (2013) A bright monomeric green fluorescent protein derived from Branchiostoma lanceolatum Nat. Methods 10, 407-409 10.1038/nmeth.2413
19. Miroux, B. and Walker, J. E. (1996) Over-production of proteins in Escherichia coli: mutant hosts that allow synthesis of some membrane proteins and globular proteins at high levels J. Mol. Biol. 260, 289-298 10.1006/jmbi.1996.0399
20. Wagner, S., Klepsch, M. M., Schlegel, S., Appel, A., Draheim, R., Tarry, M., Högbom, M., van Wijk, K. J., Slotboom, D. J., Persson, J. O., and de Gier, J.-W. (2008) Tuning Escherichia coli for membrane protein overexpression Proc. Natl. Acad. Sci. U. S. A. 105, 14371-14376 10.1073/pnas.0804090105
21. Whitmore, L. and Wallace, B. A. (2004) DICHROWEB, an online server for protein secondary structure analyses from circular dichroism spectroscopic data Nucleic Acids Res. 32, W668-W673 10.1093/nar/gkh371
22. Whitmore, L. and Wallace, B. A. (2008) Protein secondary structure analyses from circular dichroism spectroscopy: Methods and reference databases Biopolymers 89, 392-400 10.1002/bip.20853
23. Compton, L. A. and Johnson, W. C. (1986) Analysis of protein circular dichroism spectra for secondary structure using a simple matrix multiplication Anal. Biochem. 155, 155-167 10.1016/0003-2697(86)90241-1
24. Manavalan, P. and Johnson, W. C., Jr. (1987) Variable selection method improves the prediction of protein secondary structure from circular dichroism spectra Anal. Biochem. 167, 76-85 10.1016/0003-2697(87)90135-7
25. Sreerama, N. and Woody, R. W. (2000) Estimation of Protein Secondary Structure from Circular Dichroism Spectra: Comparison of CONTIN, SELCON, and CDSSTR Methods with an Expanded Reference Set Anal. Biochem. 287, 252-260 10.1006/abio.2000.4880
26. McDonald, J. (2015) Handbook of Biological Statistics, Sparky House Publishing.
27. Jones, D. T. (1999) Protein secondary structure prediction based on position-specific scoring matrices J. Mol. Biol. 292, 195-202 10.1006/jmbi.1999.3091
28. Buchan, D. W. A., Minneci, F., Nugent, T. C. O., Bryson, K., and Jones, D. T. (2013) Scalable web services for the PSIPRED Protein Analysis Workbench Nucleic Acids Res. 41, W349-357 10.1093/nar/gkt381
29. Witholt, B., Boekhout, M., Brock, M., Kingma, J., Heerikhuizen, H. V., and Leij, L. D. (1976) An efficient and reproducible procedure for the formation of spheroplasts from variously grown Escherichia coli Anal. Biochem. 74, 160-170 10.1016/0003-2697(76)90320-1