Abstract
The human U2B″ protein is one of the unique proteins that comprise the U2 snRNP, but it is also a representative of the U1A/U2B″ protein family. In the U2 snRNP, it is bound to Stem-Loop IV (SLIV) of the U2 snRNA. We find that in vitro it binds not only to human SLIV, but also to Stem-Loop II (SLII) from human U1 snRNA and to Drosophila U2 snRNA SLIV. The thermodynamics of these binding interactions show a striking similarity, leading to the conclusion that U2B″ has a relaxed specificity for its RNA targets. The binding properties of U2B″ are distinct from those of human U1A and of Drosophila SNF, despite its high homology to those proteins, and so provide important new information on how this protein family has modulated its target preferences.
MeSH Terms
Amino Acid Sequence
Animals
Base Sequence
Drosophila
Humans
Models, Molecular
Molecular Sequence Data
Nucleic Acid Conformation
Protein Binding
RNA, Small Nuclear/chemistry,metabolism
Thermodynamics
snRNP Core Proteins/metabolism
Chemicals
RNA, Small Nuclear
SNRPB2 protein, human
U1 small nuclear RNA
U2 small nuclear RNA
snRNP Core Proteins
Authors & Affiliations
2 authors, click to expand affiliations / ORCID
Williams Sandra G
Department of Biochemistry and Molecular Biophysics, Washington University Medical School, St Louis, MO 63110, United States.
Hall Kathleen B
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