The Yeast hnRNP-Like Proteins Yra1p and Yra2p Participate in mRNA Export through Interaction with Mex67p

Autor: Patrizia Vinciguerra, Daniel Zenklusen, Françoise Stutz, Yvan Strahm
Jazyk: angličtina
Rok vydání: 2001
Předmět:
Nucleocytoplasmic Transport Proteins
Saccharomyces cerevisiae Proteins
RNA
Messenger/genetics/metabolism

Recombinant Fusion Proteins
Saccharomyces cerevisiae
Immunoblotting
Plasma protein binding
Fungal Proteins/chemistry/genetics/metabolism
Nuclear Proteins/chemistry/genetics/metabolism
DNA-binding protein
Recombinant Fusion Proteins/genetics/metabolism
Fungal Proteins
Transformation
Genetic

Genes
Reporter

Genes
Reporter/genetics

Nucleocytoplasmic Communication
RNA
Messenger

RNA-Binding Proteins/genetics/metabolism
Nuclear protein
Molecular Biology
Ribonucleoproteins/chemistry/genetics/metabolism
Genetics
Messenger RNA
biology
RNA
Nuclear Proteins
RNA-Binding Proteins
RNA
Fungal

Cell Biology
biology.organism_classification
Plasmids/genetics/metabolism
In vitro
Cell biology
Protein Structure
Tertiary

Ribonucleoproteins
Saccharomyces cerevisiae/genetics/metabolism
RNA
Fungal/metabolism

Plasmids
Protein Binding
Zdroj: Molecular and Cellular Biology, Vol. 21, No 13 (2001) pp. 4219-32
ISSN: 0270-7306
Popis: Yra1p is an essential nuclear protein which belongs to the evolutionarily conserved REF (RNA and export factor binding proteins) family of hnRNP-like proteins. Yra1p contributes to mRNA export in vivo and directly interacts with RNA and the shuttling mRNP export receptor Mex67p in vitro. Here we describe a second nonessential Saccharomyces cerevisiae family member, called Yra2p, which is able to complement a YRA1 deletion when overexpressed. Like other REF proteins, Yra1p and Yra2p consist of two highly conserved N- and C-terminal boxes and a central RNP-like RNA-binding domain (RBD). These conserved regions are separated by two more variable regions, N-vr and C-vr. Surprisingly, the deletion of a single conserved box or the deletion of the RBD in Yra1p does not affect viability. Consistently, neither the conserved N and C boxes nor the RBD is required for Mex67p and RNA binding in vitro. Instead, the N-vr and C-vr regions both interact with Mex67p and RNA. We further show that Yra1 deletion mutants which poorly interact with Mex67p in vitro affect the association of Mex67p with mRNP complexes in vivo and are paralleled by poly(A)(+) RNA export defects. These observations support the idea that Yra1p promotes mRNA export by facilitating the recruitment of Mex67p to the mRNP.
Databáze: OpenAIRE