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Structure of the nuclear factor ALY: insights into post-transcriptional regulatory and mRNA nuclear export processes.

Abstract：

:ALY is a ubiquitously expressed nuclear protein which interacts with proteins such as TAP that are involved in export of mRNA from the nucleus to the cytoplasm, as well as with proteins that bind the T cell receptor alpha gene enhancer. ALY has also been shown to bind mRNA and to co-localize in the nucleus with components of a multiprotein postsplicing complex that is deposited 20-24 nucleotides upstream of exon-exon junctions. ALY has a conserved RNA binding domain (RBD) flanked by Gly-Arg rich N-terminal and C-terminal sequences. We determined the solution structure of the RBD homology region in ALY by nuclear magnetic resonance methods. The RBD motif in ALY has a characteristic beta(1)alpha(1)beta(2)-beta(3)alpha(2)beta(4) fold, consisting of a beta sheet composed of four antiparallel beta strands and two alpha helices that pack on one face of the beta sheet. As in other RBD structures, the beta sheet has an exposed face with hydrophobic and charged residues that could modulate interactions with other molecules. The loop that connects beta strands 2 and 3 is in intermediate motion in the NMR time scale, which is also characteristic of other RBDs. This loop presents side chains close to the exposed surface of the beta sheet and is a primary candidate site for intermolecular interactions. The structure of the conserved RBD of ALY provides insight into the nature of interactions involving this multifunctional protein.

journal_name

Biochemistry

journal_title

Biochemistry

authors

Pérez-Alvarado GC,Martínez-Yamout M,Allen MM,Grosschedl R,Dyson HJ,Wright PE

doi

10.1021/bi034062o

subject

Has Abstract

pub_date

2003-06-24 00:00:00

pages

7348-57

issue

24

eissn

0006-2960

issn

1520-4995

journal_volume

42

pub_type

杂志文章

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