Capture of unstable protein complex on the streptavidin-coated single-walled carbon nanotubes
Source abstract
Abstract
Purification of unstable protein complexes is a bottleneck for investigation of their 3D structure and in protein–protein interaction studies. In this paper, we demonstrate that streptavidin-coated single-walled carbon nanotubes (Strep•SWNT) can be used to capture the biotinylated DNA–EcoRI complexes on a 2D surface and in solution using atomic force microscopy and electrophoresis analysis, respectively. The restriction enzyme EcoRI forms unstable complexes with DNA in the absence of Mg2+. Capturing the EcoRI–DNA complexes on the Strep•SWNT succeeded in the absence of Mg2+, demonstrating that the Strep•SWNT can be used for purifying unstable protein complexes.
Source: openaire · Quality: candidate unverified · Source record ↗
Research context
OpenAlex topics: Nanopore and Nanochannel Transport Studies · Carbon Nanotubes in Composites · Biotin and Related Studies
SciVX discovery tags are terminology-based. OpenAlex topics are source-provided classifications.
References (18)
Show source-provided references
1. Austin RJ, Biggin MD (1996) Purification of the Drosophila RNA polymerase II general transcription factors. Proc Natl Acad Sci USA 93:5788–579210.1073/pnas.93.12.5788 ↗
2. Berggard T, Linse S, James P (2007) Methods for the detection and analysis of protein–protein interactions. Proteomics 7:2833–284210.1002/pmic.200700131 ↗
3. Burckstummer T, Bennett KL, Preradovic A, Schutze G, Hantschel O, Superti-Furga G, Bauch A (2006) An efficient tandem affinity purification procedure for interaction proteomics in mammalian cells. Nat Methods 3:1013–101910.1038/nmeth968 ↗
4. Chen JP (1990) Novel affinity-based processes for protein-purification. J Ferment Bioeng 70:199–20910.1016/0922-338X(90)90188-3 ↗
5. Dame RT, Goosen N (2002) HU: promoting or counteracting DNA compaction? FEBS Lett 529:151–15610.1016/S0014-5793(02)03363-X ↗
6. Frank J (2002) Single-particle imaging of macromolecules by cryo-electron microscopy. Annu Rev Biophys Biomol 31:303–31910.1146/annurev.biophys.31.082901.134202 ↗
7. Liu ZF, Galli F, Janssen KGH, Jiang LH, van der Linden HJ, de Geus DC, Voskamp P, Kuil ME, Olsthoorn RCL, Oosterkamp TH, Hankemeier T, Abrahams JP (2010a) Stable single-walled carbon nanotube–streptavidin complex for biorecognition. J Phys Chem C 114:4345–435210.1021/jp911441d ↗
8. Liu ZF, Jiang LH, Galli F, Nederlof I, Olsthoorn RCL, Lamers GEM, Oosterkamp TH, Abrahams JP (2010b) A graphene oxide•streptavidin complex for biorecognition—towards affinity purification. Adv Funct Mater 20:2857–286510.1002/adfm.201000761 ↗
9. Liu ZF, Galli F, Waterreus WJ, Meulenbroek E, Koning RI, Lamers GEM, Olsthoorn RCL, Pannu N, Oosterkamp TH, Koster AJ, Dame RT, Abrahams JP (2012) Single-walled carbon nanotubes as scaffolds to concentrate DNA for the study of DNA–protein interactions. ChemPhysChem 13:1569–157510.1002/cphc.201100896 ↗
10. Park S, Lee KS, Bozoklu G, Cai W, Nguyen ST, Ruoff RS (2008) Graphene oxide papers modified by divalent ions enhancing mechanical properties via chemical cross-linking. ACS Nano 2:572–57810.1021/nn700349a ↗
11. Phizicky EM, Fields S (1995) Protein–protein interactions—methods for detection and analysis. Microbiol Rev 59:94–12310.1128/MMBR.59.1.94-123.1995 ↗
12. Rouviereyaniv J, Gros F (1975) Characterization of a novel, low-molecular-weight DNA-binding protein from Escherichia coli. Proc Natl Acad Sci USA 72:3428–343210.1073/pnas.72.9.3428 ↗
13. Sorel I, Pietrement O, Hamon L, Baconnais S, Le Cam E, Pastre D (2006) The EcoRI–DNA complex as a model for investigating protein–DNA interactions by atomic force microscopy. Biochemistry 45:14675–1468210.1021/bi060293u ↗
14. Tao Y, Zhang W (2000) Recent developments in cryo-electron microscopy reconstruction of single particles. Curr Opin Struct Biol 10:616–62210.1016/S0959-440X(00)00139-1 ↗
15. Thomas M, Davis RW (1975) Studies on cleavage of bacteriophage-Lambda DNA with EcoRI restriction endonuclease. J Mol Biol 91:315–32010.1016/0022-2836(75)90383-6 ↗
16. van Heel M, Gowen B, Matadeen R, Orlova EV, Finn R, Pape T, Cohen D, Stark H, Schmidt R, Schatz M, Patwardhan A (2000) Single-particle electron cryo-microscopy: towards atomic resolution. Q Rev Biophys 33:307–36910.1017/S0033583500003644 ↗
17. Wagner K, Moolenaar G, van Noort J, Goosen N (2009) Single-molecule analysis reveals two separate DNA-binding domains in the Escherichia coli UvrA dimer. Nucl Acids Res 37:1962–197210.1093/nar/gkp071 ↗
18. Zhou Z (2008) Towards atomic resolution structural determination by single-particle cryo-electron microscopy. Curr Opin Struct Biol 18:218–22810.1016/j.sbi.2008.03.004 ↗