PDBsum entry 6ryi

DNA binding protein

PDB id: 6ryi

Contents

Protein chains

59 a.a.

DNA/RNA

PDB id:

6ryi

Name:

DNA binding protein

Title:

Wus-hd bound to g-box DNA

Structure:

Protein wuschel. Chain: a, b, c, d, e. Synonym: atwus,plant growth activator 6. Engineered: yes. DNA (5'- d(p Gp Tp Cp Gp Tp Cp Ap Cp Gp Tp Gp Ap Tp Gp Gp G)-3'). Chain: f, h. Engineered: yes. DNA (5'-

Source:

Arabidopsis thaliana. Thale cress. Organism_taxid: 3702. Gene: wus, pga6, at2g17950, t27k22.18. Expressed in: escherichia coli. Expression_system_taxid: 562. Synthetic: yes. Organism_taxid: 3702

Resolution:

2.69Å R-factor: 0.197 R-free: 0.251

Authors:

J.J.Sloan,K.Wild,I.Sinning

Key ref:

J.Sloan et al. (2020). Structural basis for the complex DNA binding behavior of the plant stem cell regulator WUSCHEL. Nat Commun, 11, 2223. PubMed id: 32376862 DOI: 10.1038/s41467-020-16024-y

Date:

10-Jun-19 Release date: 29-Apr-20

Protein chains

Q9SB92  (WUS_ARATH) -  Protein WUSCHEL from Arabidopsis thaliana

Seq: 292 a.a.

Struc: 59 a.a.

DNA/RNA chains

G-T-C-G-T-C-A-C-G-T-G-A-T-G-G-G 16 bases

C-C-C-A-T-C-A-C-G-T-G-A-C-G-A-C 16 bases

G-T-C-G-T-C-A-C-G-T-G-A-T-G-G 15 bases

C-A-T-C-A-C-G-T-G-A-C-G-A-C 14 bases

Enzyme reactions

• Enzyme class: E.C.?

DOI no: 10.1038/s41467-020-16024-y

Nat Commun 11:2223 (2020)

PubMed id: 32376862

Structural basis for the complex DNA binding behavior of the plant stem cell regulator WUSCHEL.

J.Sloan, J.P.Hakenjos, M.Gebert, O.Ermakova, A.Gumiero, G.Stier, K.Wild, I.Sinning, J.U.Lohmann.

ABSTRACT

Stem cells are one of the foundational evolutionary novelties that allowed the independent emergence of multicellularity in the plant and animal lineages. In plants, the homeodomain (HD) transcription factor WUSCHEL (WUS) is essential for the maintenance of stem cells in the shoot apical meristem. WUS has been reported to bind to diverse DNA motifs and to act as transcriptional activator and repressor. However, the mechanisms underlying this remarkable behavior have remained unclear. Here, we quantitatively delineate WUS binding to three divergent DNA motifs and resolve the relevant structural underpinnings. We show that WUS exhibits a strong binding preference for TGAA repeat sequences, while retaining the ability to weakly bind to TAAT elements. This behavior is attributable to the formation of dimers through interactions of specific residues in the HD that stabilize WUS DNA interaction. Our results provide a mechanistic basis for dissecting WUS dependent regulatory networks in plant stem cell control.