Electron microscopy of Chaetomium pom152 shows the assembly of ten-bead string - PubMed (original) (raw)

Electron microscopy of Chaetomium pom152 shows the assembly of ten-bead string

Qi Hao et al. Cell Discov. 2018.

No abstract available

PubMed Disclaimer

Conflict of interest statement

The authors declare that they have no conflict of interest.

Figures

Fig. 1

Fig. 1. Electron microscopy of _Ct_pom152 reveals the assembly of beaded strings.

a Domain architecture of _Ct_pom152 and _Hs_gp210. Regions without a predicted fold are indicated in gray; Ig, immunoglobulin (Ig)-like fold; TM, transmembrane segment; pre-Ig, the conserved segment between TM and Ig1. See Supplementary Figs. S1, S2 for details. b Limited chymotryptic digestion of full-length (FL) recombinant _Ct_pom152. c Negative-stain EM of chymotryptic fragment showed beaded and flexible strings of ~40 nm in length (37 ± 4 nm, number of particles: N = 30); two of the beaded strings (two dashed boxes) are shown enlarged (orange, bottom inserts); up to ten beads are discernible. d SDS-PAGE and Coomassie Blue staining of purified recombinant _Ct_pom152186-1270. e Like c, negative-stain EM of recombinant _Ct_pom152186-1270 also showed beaded string structures (measures 40 ± 5 nm, N = 30). f SEC-MALS indicates that _Ct_pom152186-1270 is a monomer. g–j Cryo-electron micrograph of _Ct_pom152FL. g Single particle showed flexible beaded strings (measures 44 ± 3 nm, N = 30), as seen in negative-stain EM (c, e) and four selected particles (orange with dashed box) are enlarged (h). i Two selected particles with high contrast showing ten beads (indicated by arrow heads) and the large structural variations. j _Ct_pom152FL polymerizes into long continuous strings with no punctuation marks. Particles represent the polymer formed by seven (bottom left), two (top), and five copies (right). k We speculate that (1) eight trans region of pom152 head-to-tail connect into a flexible ring and (2) two anti-parallel, stacked rings form above (cyan, omitted regions represented by dashed line), below (orange, omitted regions represented by dashed line), and mid-plane (black dashed line)

Similar articles

Cited by

References

    1. Akey CW, Radermacher M. Architecture of the xenopus nuclear pore complex revealed by three-dimensional cryo-electron microscopy. J. Cell. Biol. 1993;122:1–19. doi: 10.1083/jcb.122.1.1. - DOI - PMC - PubMed
    1. Kelley LA, Mezulis S, Yates CM, Wass MN, Sternberg MJ. The Phyre2 web portal for protein modeling, prediction and analysis. Nat. Protoc. 2015;10:845–858. doi: 10.1038/nprot.2015.053. - DOI - PMC - PubMed
    1. Kim SJ, et al. Integrative structure and functional anatomy of a nuclear pore complex. Nature. 2018;555:475–482. doi: 10.1038/nature26003. - DOI - PMC - PubMed
    1. Alber F, et al. The molecular architecture of the nuclear pore complex. Nature. 2007;450:695–701. doi: 10.1038/nature06405. - DOI - PubMed
    1. Mahamid J, et al. Visualizing the molecular sociology at the HeLa cell nuclear periphery. Science. 2016;351:969–972. doi: 10.1126/science.aad8857. - DOI - PubMed

LinkOut - more resources