Phosphorylation of a chloroplast RNA-binding protein changes its affinity to RNA
نویسندگان
چکیده
منابع مشابه
Phosphorylation of a chloroplast RNA-binding protein changes its affinity to RNA
An RNA-binding protein of 28 kDa (28RNP) was previously isolated from spinach chloroplasts and found to be required for 3' end-processing of chloroplast mRNAs. The amino acid sequence of 28RNP revealed two approximately 80 amino-acid RNA-binding domains, as well as an acidic- and glycine-rich amino terminal domain. Upon analysis of the RNA-binding properties of the 'native' 28RNP in comparison ...
متن کاملPhosphorylation of the RNA-dependent protein kinase regulates its RNA-binding activity.
The RNA-dependent protein kinase (PKR) is an interferon-induced, RNA-activated enzyme that phosphorylates the alpha-subunit of eukaryotic initiation factor 2 (eIF2alpha), inhibiting the function of the eIF2 complex and continued initiation of translation. When bound to an activating RNA and ATP, PKR undergoes autophosphorylation reactions at multiple serine and threonine residues. This autophos...
متن کاملChloroplast RNA-binding and pentatricopeptide repeat proteins.
Chloroplast gene expression is mainly regulated at the post-transcriptional level by numerous nuclear-encoded RNA-binding protein factors. In the present study, we focus on two RNA-binding proteins: cpRNP (chloroplast ribonucleoprotein) and PPR (pentatricopeptide repeat) protein. These are suggested to be major contributors to chloroplast RNA metabolism. Tobacco cpRNPs are composed of five diff...
متن کاملFunctional analysis of glycin rich- RNA binding protein, a suppressor of trehalose-6-phosphate mediating growth arrest in Arabidopsis thaliana
Metabolism of the alpha-1,1 glucose disaccharide, trehalose, is indispensable in plants. In the Murashigeand Skoog (MS) medium, trehalose inhibits plant growth and allocation of carbon to roots. A suppressorof trehalose-6-phosphate (T6P) mediated growth arrest, GR-RBP2, is characterized in more detail.Phylogenetic analysis revealed that GR-RBP2 is a protein of likely prokaryot...
متن کاملPhosphorylation of p68 RNA helicase regulates RNA binding by the C-terminal domain of the protein.
We previously reported ATPase, RNA unwinding, and RNA-binding activities of recombinant p68 RNA helicase that was expressed in Escherichia coli. Huang et al. The recombinant protein bound both single-stranded (ss) and double-stranded (ds) RNAs. To further characterize the substrate RNA binding by p68 RNA helicase, we expressed and purified the recombinant N-terminal and C-terminal domains of th...
متن کاملذخیره در منابع من
با ذخیره ی این منبع در منابع من، دسترسی به آن را برای استفاده های بعدی آسان تر کنید
ژورنال
عنوان ژورنال: Nucleic Acids Research
سال: 1995
ISSN: 0305-1048,1362-4962
DOI: 10.1093/nar/23.13.2506