scholarly journals Mapping of the RNA-binding and endoribonuclease domains of NIPP1, a nuclear targeting subunit of protein phosphatase 1

1999 ◽  
Vol 342 (1) ◽  
pp. 13-19 ◽  
Author(s):  
Qiming JIN ◽  
Monique BEULLENS ◽  
Izabela JAGIELLO ◽  
Aleyde VAN EYNDE ◽  
Veerle VULSTEKE ◽  
...  
Keyword(s):  
Protein Phosphatase ◽  
Rna Binding ◽  
Specific Activity ◽  
Binding Domain ◽  
Protein Phosphatase 1 ◽  
Binding Motif ◽  
Nucleic Acid Binding ◽  
Nuclear Targeting ◽  
Rna Binding Domain ◽  
Endoribonuclease Activity

NIPP1 (351 residues) is a major regulatory and RNA-anchoring subunit of protein phosphatase 1 in the nucleus. Using recombinant and synthetic fragments of NIPP1, the RNA-binding domain was mapped to the C-terminal residues 330-351. A synthetic peptide encompassing this sequence equalled intact NIPP1 in RNA-binding affinity and could be used to dissociate NIPP1 from the nuclear particulate fraction. An NIPP1 fragment consisting of residues 225-351 (Ard1/NIPP1γ), that may be encoded by an alternatively spliced transcript in transformed B-lymphocytes, displayed a single-strand Mg2+-dependent endoribonuclease activity. However, full-length NIPP1 and NIPP1143-351 were not able to cleave RNA, indicating that the endoribonuclease activity of NIPP1 is restrained by its central domain. The endoribonuclease activity was also recovered in the RNA-binding domain, NIPP1330-351, but with a 30-fold lower specific activity. Thus, the endoribonuclease catalytic site and the RNA-binding site both reside in the C-terminal 22 residues of NIPP1. The latter domain does not conform to any known nucleic-acid binding motif.

scholarly journals Mapping the RNA-binding domain on the Apple chlorotic leaf spot virus movement protein

2005 ◽  
Vol 86 (1) ◽  
pp. 225-229 ◽  
Author(s):  
Masamichi Isogai ◽  
Nobuyuki Yoshikawa
Keyword(s):  
Leaf Spot ◽  
Rna Binding ◽  
Movement Protein ◽  
Binding Domain ◽  
Sequence Specificity ◽  
Nucleic Acid Binding ◽  
Spot Virus ◽  
Uv Crosslinking ◽  
Chlorotic Leaf ◽  
Rna Binding Domain

The RNA-binding properties of the cell-to-cell movement protein (MP) of Apple chlorotic leaf spot virus were analysed. MP was expressed in Escherichia coli and was used in UV-crosslinking analysis, using a digoxigenin–UTP-labelled RNA probe and gel-retardation analysis. The analyses demonstrated that MP bound cooperatively to single-stranded RNA (ssRNA). When analysed for NaCl dependence of the RNA-binding activity, the majority of the MP could bind ssRNA even in binding buffer with 1 M NaCl. Furthermore, competition binding experiments showed that the MP bound preferentially to ssRNA and single-stranded DNA without sequence specificity. MP deletion mutants were used to identify the RNA-binding domain by UV-crosslinking analysis. Amino acid residues 82–126 and 127–287 potentially contain two independently active, single-stranded nucleic acid-binding domains.

scholarly journals Mapping of the RNA-binding and endoribonuclease domains of NIPP1, a nuclear targeting subunit of protein phosphatase 1

1999 ◽  
Vol 342 (1) ◽  
pp. 13 ◽  
Author(s):  
Qiming JIN ◽  
Monique BEULLENS ◽  
Izabela JAGIELLO ◽  
Aleyde VAN EYNDE ◽  
Veerle VULSTEKE ◽  
...  
Keyword(s):  
Protein Phosphatase ◽  
Rna Binding ◽  
Protein Phosphatase 1 ◽  
Nuclear Targeting

Transient Structural Ordering of the RNA-Binding Domain of Carnation Mottle Virus p7 Movement Protein Modulates Nucleic Acid Binding

ChemBioChem ◽  
2005 ◽  
Vol 6 (8) ◽  
pp. 1391-1396 ◽  
Author(s):  
Marçal Vilar ◽  
Ana Saurí ◽  
Jose F. Marcos ◽  
Ismael Mingarro ◽  
Enrique Pérez-Payá
Keyword(s):  
Nucleic Acid ◽  
Rna Binding ◽  
Movement Protein ◽  
Binding Domain ◽  
Mottle Virus ◽  
Nucleic Acid Binding ◽  
Structural Ordering ◽  
Rna Binding Domain ◽  
Carnation Mottle Virus

scholarly journals The Solution Structure of the S1 RNA Binding Domain: A Member of an Ancient Nucleic Acid–Binding Fold

Cell ◽  
1997 ◽  
Vol 88 (2) ◽  
pp. 235-242 ◽  
Author(s):  
Mark Bycroft ◽  
Tim J.P Hubbard ◽  
Mark Proctor ◽  
Stefan M.V Freund ◽  
Alexey G Murzin
Keyword(s):  
Nucleic Acid ◽  
Solution Structure ◽  
Rna Binding ◽  
Binding Domain ◽  
Nucleic Acid Binding ◽  
Rna Binding Domain

scholarly journals Targeting Protein Phosphatase 1 (PP1) to the Actin Cytoskeleton: the Neurabin I/PP1 Complex Regulates Cell Morphology

2002 ◽  
Vol 22 (13) ◽  
pp. 4690-4701 ◽  
Author(s):  
Carey J. Oliver ◽  
Ryan T. Terry-Lorenzo ◽  
Elizabeth Elliott ◽  
Wendy A. Christensen Bloomer ◽  
Shi Li ◽  
...  
Keyword(s):  
Protein Kinase ◽  
Actin Cytoskeleton ◽  
Protein Phosphatase ◽  
Binding Domain ◽  
Stress Fibers ◽  
Protein Phosphatase 1 ◽  
In Vivo Studies ◽  
Actin Binding ◽  
Binding Motif ◽  
Actin Binding Domain

ABSTRACT Neurabin I, a neuronal actin-binding protein, binds protein phosphatase 1 (PP1) and p70 ribosomal S6 protein kinase (p70S6K), both proteins implicated in cytoskeletal dynamics. We expressed wild-type and mutant neurabins fused to green fluorescent protein in Cos7, HEK293, and hippocampal neurons. Biochemical and cellular studies showed that an N-terminal F-actin-binding domain dictated neurabin I localization at actin cytoskeleton and promoted disassembly of stress fibers. Deletion of the C-terminal coiled-coil and sterile alpha motif domains abolished neurabin I dimerization and induced filopodium extension. Immune complex assays showed that neurabin I recruited an active PP1 via a PP1-docking sequence,457KIKF460. Mutation of the PP1-binding motif or PP1 inhibition by okadaic acid and calyculin A abolished filopodia and restored stress fibers in cells expressing neurabin I. In vitro and in vivo studies suggested that the actin-binding domain attenuated protein kinase A (PKA) phosphorylation of neurabin I. Modification of a major PKA site, serine-461, impaired PP1 binding. Finally, p70S6K was excluded from neurabin I/PP1 complexes and required the displacement of PP1 for recruitment to neurabin I. These studies provided new insights into the assembly and regulation of a neurabin I/PP1 complex that controls actin rearrangement to promote spine development in mammalian neurons.

scholarly journals Requirement for C-terminal Extension to the RNA Binding Domain for Efficient RNA Binding by Ribosomal Protein L2

2002 ◽  
Vol 66 (3) ◽  
pp. 682-684 ◽  
Author(s):  
Takeshi HAYASHI ◽  
Maino TAHARA ◽  
Kenta IWASAKI ◽  
Yoshiaki KOUZUMA ◽  
Makoto KIMURA
Keyword(s):  
Ribosomal Protein ◽  
Rna Binding ◽  
Binding Domain ◽  
Ribosomal Protein L2 ◽  
Rna Binding Domain
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