scholarly journals Isolation of small RNA-binding proteins fromE. coli: Evidence for frequent interaction of RNAs with RNA polymerase

RNA Biology ◽  
2008 ◽  
Vol 5 (1) ◽  
pp. 30-40 ◽  
Author(s):  
Nikolai Windbichler ◽  
Frederike von Pelchrzim ◽  
Oliver Mayer ◽  
Edina Csaszar ◽  
Renée Schroeder
RNA ◽  
2007 ◽  
Vol 13 (3) ◽  
pp. 361-373 ◽  
Author(s):  
K. L. Carroll ◽  
R. Ghirlando ◽  
J. M. Ames ◽  
J. L. Corden

2014 ◽  
Vol 3 (6) ◽  
pp. 950-960 ◽  
Author(s):  
Jonathan Osborne ◽  
Louise Djapgne ◽  
Bao Quoc Tran ◽  
Young Ah Goo ◽  
Amanda G. Oglesby‐Sherrouse

Nature Plants ◽  
2021 ◽  
Vol 7 (3) ◽  
pp. 342-352
Author(s):  
Baoye He ◽  
Qiang Cai ◽  
Lulu Qiao ◽  
Chien-Yu Huang ◽  
Shumei Wang ◽  
...  

Reproduction ◽  
2011 ◽  
Vol 142 (6) ◽  
pp. 803-817 ◽  
Author(s):  
Mai Nguyen-Chi ◽  
Dominique Morello

Changes in mRNA translation and degradation represent post-transcriptional processes operating during gametogenesis and early embryogenesis to ensure regulated protein synthesis. Numerous mRNA-binding proteins (RBPs) have been described in multiple animal models that contribute to the control of mRNA translation and decay during oogenesis and spermatogenesis. An emerging view from studies performed in germ cells and somatic cells is that RBPs associate with their target mRNAs in RNA–protein (or ribonucleoprotein) complexes (mRNPs) that assemble in various cytoplasmic RNA granules that communicate with the translation machinery and control mRNA storage, triage, and degradation. In comparison withXenopus, Caenorhabditis elegans, orDrosophila, the composition and role of cytoplasmic RNA-containing granules in mammalian germ cells are still poorly understood. However, regained interest for these structures has emerged with the recent discovery of their role in small RNA synthesis and transposon silencing through DNA methylation. In this review, we will briefly summarize our current knowledge on cytoplasmic RNA granules in murine germ cells and describe the role of some of the RBPs they contain in regulating mRNA metabolism and small RNA processing during gametogenesis.


Genetics ◽  
2000 ◽  
Vol 154 (2) ◽  
pp. 557-571 ◽  
Author(s):  
Nicholas K Conrad ◽  
Scott M Wilson ◽  
Eric J Steinmetz ◽  
Meera Patturajan ◽  
David A Brow ◽  
...  

Abstract Recent evidence suggests a role for the carboxyl-terminal domain (CTD) of the largest subunit of RNA polymerase II (pol II) in pre-mRNA processing. The yeast NRD1 gene encodes an essential RNA-binding protein that shares homology with mammalian CTD-binding proteins and is thought to regulate mRNA abundance by binding to a specific cis-acting element. The present work demonstrates genetic and physical interactions among Nrd1p, the pol II CTD, Nab3p, and the CTD kinase CTDK-I. Previous studies have shown that Nrd1p associates with the CTD of pol II in yeast two-hybrid assays via its CTD-interaction domain (CID). We show that nrd1 temperature-sensitive alleles are synthetically lethal with truncation of the CTD to 9 or 10 repeats. Nab3p, a yeast hnRNP, is a high-copy suppressor of some nrd1 temperature-sensitive alleles, interacts with Nrd1p in a yeast two-hybrid assay, and coimmunoprecipitates with Nrd1p. Temperature-sensitive alleles of NAB3 are suppressed by deletion of CTK1, a kinase that has been shown to phosphorylate the CTD and increase elongation efficiency in vitro. This set of genetic and physical interactions suggests a role for yeast RNA-binding proteins in transcriptional regulation.


Nature Plants ◽  
2021 ◽  
Author(s):  
Baoye He ◽  
Qiang Cai ◽  
Lulu Qiao ◽  
Chien-Yu Huang ◽  
Shumei Wang ◽  
...  

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