PDBsum entry 1x0f

Transcription/DNA

PDB id: 1x0f

Contents

Protein chain

79 a.a. *

DNA/RNA

* Residue conservation analysis

PDB id:

1x0f

Name:

Transcription/DNA

Title:

Complex structure of thE C-terminal RNA-binding domain of hnrnp d(auf1) with telomeric DNA

Structure:

5'-d(p Tp Ap Gp G)-3'. Chain: b. Engineered: yes. Heterogeneous nuclear ribonucleoprotein d0. Chain: a. Fragment: c-terminal RNA-binding domain. Synonym: hnrnp d0, au-rich element RNA-binding protein 1. Engineered: yes

Source:

Synthetic: yes. Homo sapiens. Human. Organism_taxid: 9606. Expressed in: escherichia coli bl21(de3). Expression_system_taxid: 469008.

NMR struc:

20 models

Authors:

Y.Enokizono,Y.Konishi,K.Nagata,K.Ouhashi,S.Uesugi,F.Ishikawa, M.Katahira

Key ref:

Y.Enokizono et al. (2005). Structure of hnRNP D complexed with single-stranded telomere DNA and unfolding of the quadruplex by heterogeneous nuclear ribonucleoprotein D. J Biol Chem, 280, 18862-18870. PubMed id: 15734733 DOI: 10.1074/jbc.M411822200

Date:

22-Mar-05 Release date: 05-Apr-05

Protein chain

Q14103  (HNRPD_HUMAN) -  Heterogeneous nuclear ribonucleoprotein D0 from Homo sapiens

Seq: 355 a.a.

Struc: 79 a.a.

DNA/RNA chain

T-A-G-G 4 bases

Enzyme reactions

• Enzyme class: E.C.?

DOI no: 10.1074/jbc.M411822200

J Biol Chem 280:18862-18870 (2005)

PubMed id: 15734733

Structure of hnRNP D complexed with single-stranded telomere DNA and unfolding of the quadruplex by heterogeneous nuclear ribonucleoprotein D.

Y.Enokizono, Y.Konishi, K.Nagata, K.Ouhashi, S.Uesugi, F.Ishikawa, M.Katahira.

ABSTRACT

Heterogeneous nuclear ribonucleoprotein D, also known as AUF1, has two DNA/RNA-binding domains, each of which can specifically bind to single-stranded d(TTAGGG)n, the human telomeric repeat. Here, the structure of the C-terminal-binding domain (BD2) complexed with single-stranded d(TTAGGG) determined by NMR is presented. The structure has revealed that each residue of the d(TAG) segment is recognized by BD2 in a base-specific manner. The interactions deduced from the structure have been confirmed by gel retardation experiments with mutant BD2 and DNA. It is known that single-stranded DNA with the telomeric repeat tends to form a quadruplex and that the quadruplex has an inhibitory effect on telomere elongation by telomerase. This time it is revealed that BD2 unfolds the quadruplex of such DNA upon binding. Moreover, the effect of BD2 on the elongation by telomerase was examined in vitro. These results suggest the possible involvement of heterogeneous nuclear ribonucleoprotein D in maintenance of the telomere 3'-overhang either through protection of a single-stranded DNA or destabilization of the potentially deleterious quadruplex structure for the elongation by telomerase.

Selected figure(s)

Figure 3.
FIG. 3. Details of the recognition of Thy-2 (A), Ade-3 (B), and Gua-4 (C) of d(TTAGGG) by hnRNP D BD2. Hydrogen bonds are indicated by dotted lines.

Figure 4.
FIG. 4. Gel retardation experiments with mutant hnRNP D BD2s. A, Cy5-labeled d(GTCTTAGGGCGA) was incubated with either the wild type or mutant BD2 and then run on polyacrylamide gel. B, the intensity of the complex band relative to that for wild type BD2 is quantified for each mutant BD2. The results of three independent experiments were averaged.

The above figures are reprinted by permission from the ASBMB: J Biol Chem (2005, 280, 18862-18870) copyright 2005.

Figures were selected by the author.