Limits...
The pentameric nucleoplasmin fold is present in Drosophila FKBP39 and a large number of chromatin-related proteins.

Edlich-Muth C, Artero JB, Callow P, Przewloka MR, Watson AA, Zhang W, Glover DM, Debski J, Dadlez M, Round AR, Forsyth VT, Laue ED - J. Mol. Biol. (2015)

Bottom Line: The pentameric core domain, a doughnut-like structure with a central pore, is only found in the nucleoplasmin family.Furthermore, we show that two other chromatin proteins, Arabidopsis thaliana histone deacetylase type 2 (HD2) and Saccharomyces cerevisiae Fpr4, share the NPL fold and form pentamers, or a dimer of pentamers in the case of HD2.Thus, we propose a new family of proteins that share the pentameric nucleoplasmin-like NPL domain and are found in protists, fungi, plants and animals.

View Article: PubMed Central - PubMed

Affiliation: Department of Biochemistry, University of Cambridge, 80 Tennis Court Road, CB2 1GA Cambridge, United Kingdom.

Show MeSH
SANS of the NPL domain of FKBP39. (a) The scattering profile, (b) resulting distance distribution and (c) a beads model based on these data. The model was fitted with 5-fold symmetry. The data were collected on a deuterated sample of FKBP39. Each sphere of the model has a radius of 1.4 Å.
© Copyright Policy - CC BY
Related In: Results  -  Collection

License
getmorefigures.php?uid=PMC4414354&req=5

f0020: SANS of the NPL domain of FKBP39. (a) The scattering profile, (b) resulting distance distribution and (c) a beads model based on these data. The model was fitted with 5-fold symmetry. The data were collected on a deuterated sample of FKBP39. Each sphere of the model has a radius of 1.4 Å.

Mentions: Size-exclusion chromatography gave an early indication that the NPL domain forms an oligomer, and the apparent molecular weight was consistent with the formation of a nucleoplasmin-like pentamer. In order to test this hypothesis, we studied deuterated NPL using small-angle neutron scattering (SANS). The SANS scattering profile matched a protein of about 50 kDa and produced an excellent fit when modelled with 5-fold symmetry. Modelling with a 6-fold symmetry did not fit the data so well. A bead model was constructed from the scattering profile (Fig. 3), and this clearly shows a doughnut-shaped structure that matches the dimensions of the nucleoplasmin pentamer.


The pentameric nucleoplasmin fold is present in Drosophila FKBP39 and a large number of chromatin-related proteins.

Edlich-Muth C, Artero JB, Callow P, Przewloka MR, Watson AA, Zhang W, Glover DM, Debski J, Dadlez M, Round AR, Forsyth VT, Laue ED - J. Mol. Biol. (2015)

SANS of the NPL domain of FKBP39. (a) The scattering profile, (b) resulting distance distribution and (c) a beads model based on these data. The model was fitted with 5-fold symmetry. The data were collected on a deuterated sample of FKBP39. Each sphere of the model has a radius of 1.4 Å.
© Copyright Policy - CC BY
Related In: Results  -  Collection

License
Show All Figures
getmorefigures.php?uid=PMC4414354&req=5

f0020: SANS of the NPL domain of FKBP39. (a) The scattering profile, (b) resulting distance distribution and (c) a beads model based on these data. The model was fitted with 5-fold symmetry. The data were collected on a deuterated sample of FKBP39. Each sphere of the model has a radius of 1.4 Å.
Mentions: Size-exclusion chromatography gave an early indication that the NPL domain forms an oligomer, and the apparent molecular weight was consistent with the formation of a nucleoplasmin-like pentamer. In order to test this hypothesis, we studied deuterated NPL using small-angle neutron scattering (SANS). The SANS scattering profile matched a protein of about 50 kDa and produced an excellent fit when modelled with 5-fold symmetry. Modelling with a 6-fold symmetry did not fit the data so well. A bead model was constructed from the scattering profile (Fig. 3), and this clearly shows a doughnut-shaped structure that matches the dimensions of the nucleoplasmin pentamer.

Bottom Line: The pentameric core domain, a doughnut-like structure with a central pore, is only found in the nucleoplasmin family.Furthermore, we show that two other chromatin proteins, Arabidopsis thaliana histone deacetylase type 2 (HD2) and Saccharomyces cerevisiae Fpr4, share the NPL fold and form pentamers, or a dimer of pentamers in the case of HD2.Thus, we propose a new family of proteins that share the pentameric nucleoplasmin-like NPL domain and are found in protists, fungi, plants and animals.

View Article: PubMed Central - PubMed

Affiliation: Department of Biochemistry, University of Cambridge, 80 Tennis Court Road, CB2 1GA Cambridge, United Kingdom.

Show MeSH