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PMID: 10220389 Published · ppublish English Journal Article Research Support, Non-U.S. Gov't Research Support, U.S. Gov't, Non-P.H.S. Research Support, U.S. Gov't, P.H.S.

Absence of interdomain contacts in the crystal structure of the RNA recognition motifs of Sex-lethal.

Crowder SM, Kanaar R, Rio DC, Alber T

Abstract

By binding specific RNA transcripts, the Sex-lethal protein (SXL) governs sexual differentiation and dosage compensation in Drosophila melanogaster. To investigate the basis for RNA binding specificity, we determined the crystal structure of the tandem RNA recognition motifs (RRMs) of SXL. Both RRMs adopt the canonical RRM fold, and the 10-residue, interdomain linker shows significant disorder. In contrast to the previously determined structure of the two-RRM fragment of heterogeneous nuclear ribonucleoprotein Al, SXL displays no interdomain contacts between RRMs. These results suggest that the SXL RRMs are flexibly tethered in solution, and RNA binding restricts the orientation of RRMs. Therefore, the observed specificity for single-stranded, U-rich sequences does not arise from a predefined, rigid architecture of the isolated SXL RRMs.

MeSH Terms
Animals Binding Sites Drosophila Proteins Drosophila melanogaster Insect Hormones/chemistry,metabolism Molecular Sequence Data Protein Conformation RNA-Binding Proteins/chemistry,metabolism
Chemicals
Drosophila Proteins Insect Hormones RNA-Binding Proteins Sxl protein, Drosophila
Authors & Affiliations
4 authors, click to expand affiliations / ORCID
Crowder S M
Department of Molecular and Cell Biology, University of California, Berkeley, CA 94720, USA.
Kanaar R
Rio D C
Alber T
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Article Info
Journal
Proceedings of the National Academy of Sciences of the United States of America
Abbr.
Proc Natl Acad Sci U S A
ISSN
0027-8424
Published
1999-04-27
Pages
4892-7
Language
English
Region
United States
NLM ID
7505876
PMCID
PMC21787
Subset
IM
Grants
NIGMS NIH HHS · GM54793 · United States
NIGMS NIH HHS · GM56979 · United States
NICHD NIH HHS · HD28063 · United States
Databases
PDB
Analysis Services
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