Functionally conserved RNA-binding and protein-protein interaction properties of LINE-ORF1p in an ancient clade of non-LTR retrotransposons of Entamoeba histolytica

2017 ◽  
Vol 211 ◽  
pp. 84-93 ◽  
Author(s):  
Amit Kumar Gaurav ◽  
Jitender Kumar ◽  
Mridula Agrahari ◽  
Alok Bhattacharya ◽  
Vijay Pal Yadav ◽  
...  
Keyword(s):  
Entamoeba Histolytica ◽  
Protein Interaction ◽  
Rna Binding ◽  
Ltr Retrotransposons ◽  
Protein Protein Interaction

scholarly journals Mutational Definition of RNA-binding and Protein-Protein Interaction Domains of Heterogeneous Nuclear RNP C1

2000 ◽  
Vol 276 (10) ◽  
pp. 7681-7688 ◽  
Author(s):  
Lili Wan ◽  
Jeong-Kook Kim ◽  
Victoria W. Pollard ◽  
Gideon Dreyfuss
Keyword(s):  
Protein Interaction ◽  
Rna Binding ◽  
Protein Protein Interaction ◽  
Interaction Domains ◽  
Definition Of

scholarly journals A RanBP2-type zinc finger protein functions in intron splicing in Arabidopsis mitochondria and is involved in the biogenesis of respiratory complex I

2021 ◽  
Vol 49 (6) ◽  
pp. 3490-3506
Author(s):  
Stéphane Bentolila ◽  
Andrew B Gipson ◽  
Alexander J Kehl ◽  
Lauren N Hamm ◽  
Michael L Hayes ◽  
...  
Keyword(s):  
Zinc Finger ◽  
Protein Interaction ◽  
Complex I ◽  
Rna Binding ◽  
Zinc Finger Protein ◽  
Respiratory Pathway ◽  
Protein Protein Interaction ◽  
Protein Functions ◽  
Abscisic Acid Insensitive3 ◽  
Biochemical Analyses

Abstract The RanBP2 zinc finger (Znf) domain is a prevalent domain that mediates protein interaction and RNA binding. In Arabidopsis, a clade of four RanBP2 Znf-containing proteins, named the Organelle Zinc (OZ) finger family, are known or predicted to be targeted to either the mitochondria or the plastids. Previously we reported that OZ1 is absolutely required for the editing of 14 sites in chloroplasts. We now have investigated the function of OZ2, whose null mutation is embryo lethal. We rescued the null mutant by expressing wild-type OZ2 under the control of the seed-specific ABSCISIC ACID-INSENSITIVE3 (ABI3) promoter. Rescued mutant plants exhibit severely delayed development and a distinctive morphological phenotype. Genetic and biochemical analyses demonstrated that OZ2 promotes the splicing of transcripts of several mitochondrial nad genes and rps3. The splicing defect of nad transcripts results in the destabilization of complex I, which in turn affects the respiratory ability of oz2 mutants, turning on the alternative respiratory pathway, and impacting the plant development. Protein-protein interaction assays demonstrated binding of OZ2 to several known mitochondrial splicing factors targeting the same splicing events. These findings extend the known functional repertoire of the RanBP2 zinc finger domain in nuclear splicing to include plant organelle splicing.

Two families of RNA binding proteins from Trypanosoma brucei associate in a direct protein–protein interaction

2002 ◽  
Vol 122 (1) ◽  
pp. 81-89 ◽  
Author(s):  
Joseph S Pitula ◽  
Jeong Park ◽  
Marilyn Parsons ◽  
William T Ruyechan ◽  
Noreen Williams
Keyword(s):  
Trypanosoma Brucei ◽  
Protein Interaction ◽  
Binding Proteins ◽  
Rna Binding ◽  
Rna Binding Proteins ◽  
Protein Protein Interaction
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