Posttranscriptional regulation and RNA binding proteins in development

1995 ◽  
Vol 2 (4) ◽  
pp. 293-301 ◽  
Author(s):  
Susan R. Haynes
Keyword(s):  
Posttranscriptional Regulation ◽  
Binding Proteins ◽  
Rna Binding ◽  
Rna Binding Proteins

scholarly journals Posttranscriptional regulation of lipid metabolism by non-coding RNAs and RNA binding proteins

2018 ◽  
Vol 81 ◽  
pp. 129-140 ◽  
Author(s):  
Abhishek K. Singh ◽  
Binod Aryal ◽  
Xinbo Zhang ◽  
Yuhua Fan ◽  
Nathan L. Price ◽  
...  
Keyword(s):  
Lipid Metabolism ◽  
Posttranscriptional Regulation ◽  
Binding Proteins ◽  
Rna Binding ◽  
Rna Binding Proteins ◽  
Non Coding Rnas

scholarly journals Primary and Secondary Sequence Structure Requirements for Recognition and Discrimination of Target RNAs by Pseudomonas aeruginosa RsmA and RsmF

2016 ◽  
Vol 198 (18) ◽  
pp. 2458-2469 ◽  
Author(s):  
Kayley H. Schulmeyer ◽  
Manisha R. Diaz ◽  
Thomas B. Bair ◽  
Wes Sanders ◽  
Cindy J. Gode ◽  
...  
Keyword(s):  
Pseudomonas Aeruginosa ◽  
Binding Sites ◽  
Posttranscriptional Regulation ◽  
Binding Proteins ◽  
Rna Binding ◽  
Rna Binding Proteins ◽  
Consensus Sequence ◽  
Stem Loop ◽  
Content Type

ABSTRACTCsrA family RNA-binding proteins are widely distributed in bacteria and regulate gene expression at the posttranscriptional level.Pseudomonas aeruginosahas a canonical member of the CsrA family (RsmA) and a novel, structurally distinct variant (RsmF). To better understand RsmF binding properties, we performed parallel systematic evolution of ligands by exponential enrichment (SELEX) experiments for RsmA and RsmF. The initial target library consisted of 62-nucleotide (nt) RNA transcripts with central cores randomized at 15 sequential positions. Most targets selected by RsmA and RsmF were the expected size and shared a common consensus sequence (CANGGAYG) that was positioned in a hexaloop region of the stem-loop structure. RsmA and RsmF also selected for longer targets (≥96 nt) that were likely generated by rare PCR errors. Most of the long targets contained two consensus-binding sites. Representative short (single consensus site) and long (two consensus sites) targets were tested for RsmA and RsmF binding. Whereas RsmA bound the short targets with high affinity, RsmF was unable to bind the same targets. RsmA and RsmF both bound the long targets. Mutation of either consensus GGA site in the long targets reduced or eliminated RsmF binding, suggesting a requirement for two tandem binding sites. Conversely, RsmA bound long targets containing only a single GGA site with unaltered affinity. The RsmF requirement for two binding sites was confirmed withtssA1, anin vivoregulatory target of RsmA and RsmF. Our findings suggest that RsmF binding requires two GGA-containing sites, while RsmA binding requirements are less stringent.IMPORTANCEThe CsrA family of RNA-binding proteins is widely conserved in bacteria and plays important roles in the posttranscriptional regulation of protein synthesis.P. aeruginosahas two CsrA proteins, RsmA and RsmF. Although RsmA and RsmF share a few RNA targets, RsmF is unable to bind to other targets recognized by RsmA. The goal of the present study was to better understand the basis for differential binding by RsmF. Our data indicate that RsmF binding requires target RNAs with two consensus-binding sites, while RsmA recognizes targets with just a single binding site. This information should prove useful to future efforts to define the RsmF regulon and its contribution toP. aeruginosaphysiology and virulence.

scholarly journals Minireview: Posttranscriptional Regulation of the Insulin and Insulin-Like Growth Factor Systems

Endocrinology ◽  
2009 ◽  
Vol 151 (4) ◽  
pp. 1403-1408 ◽  
Author(s):  
Eun Kyung Lee ◽  
Myriam Gorospe
Keyword(s):  
Glucose Homeostasis ◽  
Posttranscriptional Regulation ◽  
Binding Proteins ◽  
Rna Binding ◽  
Rna Binding Proteins ◽  
Glucose Levels ◽  
Igf Receptors ◽  
The Stability ◽  
Mrna Binding

Insulin and IGFs share structural similarities and regulate metabolic processes including glucose homeostasis. Acute alterations in glucose levels trigger rapid changes in insulin concentration and insulin signaling. These processes are tightly regulated by posttranscriptional mechanisms that alter the stability and translation of mRNAs encoding insulin and the insulin receptor. Long-term glucose homeostasis is also modulated by IGFs and IGF receptors, whose expression is likewise subject to changes in the stability and translation of the encoding mRNAs. The control of mRNA half-life and translation is governed by RNA-binding proteins and microRNAs that interact with target transcripts at the 3′ and 5′ untranslated regions. In this review, we describe the RNA-binding proteins and microRNAs that target the mRNAs encoding insulin, IGFs, and their receptors. We discuss how these mRNA-binding factors help to elicit timely, versatile, and tissue-specific changes in insulin and IGF function, thereby effecting critical control of energy metabolism.

HuR and other turnover- and translation-regulatory RNA-binding proteins: implications for the kidney

2014 ◽  
Vol 306 (6) ◽  
pp. F569-F576 ◽  
Author(s):  
Rudolf Pullmann ◽  
Hamid Rabb
Keyword(s):  
Posttranscriptional Regulation ◽  
Binding Proteins ◽  
Rna Binding ◽  
Rna Binding Proteins ◽  
Current Knowledge ◽  
Regulation Of Gene Expression ◽  
Regulatory Elements ◽  
Matrix Remodeling ◽  
Acid Base Balance ◽  
Renal Metabolism

The posttranscriptional regulation of gene expression occurs through cis RNA regulatory elements by the action of trans factors, which are represented by noncoding RNAs (especially microRNAs) and turnover- and translation-regulatory (TTR) RNA-binding proteins (RBPs). These multifactorial proteins are a group of heterogeneous RBPs primarily implicated in controlling the decay and translation rates of target mRNAs. TTR-RBPs usually shuttle between cellular compartments (the nucleus and cytoplasm) in response to various stimuli and undergo posttranslational modifications such as phosphorylation or methylation to ensure their proper subcellular localization and function. TTR-RBPs are emerging as key regulators of a wide variety of genes influencing kidney physiology and pathology. This review summarizes the current knowledge of TTR-RBPs that influence renal metabolism. We will discuss the role of TTR-RBPs as regulators of kidney ischemia, fibrosis and matrix remodeling, angiogenesis, membrane transport, immunity, vascular tone, hypertension, and acid-base balance as well as anemia, bone mineral disease, and vascular calcification.

scholarly journals Posttranscriptional regulation by RNA-binding proteins during epithelial-to-mesenchymal transition

2013 ◽  
Vol 70 (23) ◽  
pp. 4463-4477 ◽  
Author(s):  
Luis A. Aparicio ◽  
Vanessa Abella ◽  
Manuel Valladares ◽  
Angélica Figueroa
Keyword(s):  
Posttranscriptional Regulation ◽  
Binding Proteins ◽  
Epithelial To Mesenchymal Transition ◽  
Rna Binding ◽  
Rna Binding Proteins ◽  
Mesenchymal Transition

Posttranscriptional Regulation and RNA Binding Proteins in Development

1995 ◽  
Vol 2 (4) ◽  
pp. 293-301
Author(s):  
Susan R. Haynes
Keyword(s):  
Posttranscriptional Regulation ◽  
Binding Proteins ◽  
Rna Binding ◽  
Rna Binding Proteins

scholarly journals Calreticulin Interacts with C/EBPα and C/EBPβ mRNAs and Represses Translation of C/EBP Proteins

2002 ◽  
Vol 22 (20) ◽  
pp. 7242-7257 ◽  
Author(s):  
Lubov T. Timchenko ◽  
Polina Iakova ◽  
Alana L. Welm ◽  
Z.-J. Cai ◽  
Nikolai A. Timchenko
Keyword(s):  
Rna Processing ◽  
Posttranscriptional Regulation ◽  
Binding Proteins ◽  
Rna Binding ◽  
Rna Binding Proteins ◽  
Posttranscriptional Control ◽  
Multifunctional Protein ◽  
Virus Rna

ABSTRACT We previously identified an RNA binding protein, CUGBP1, which binds to GCN repeats located within the 5′ region of C/EBPβ mRNAs and regulates translation of C/EBPβ isoforms. To further investigate the role of RNA binding proteins in the posttranscriptional control of C/EBP proteins, we purified additional RNA binding proteins that interact with GC-rich RNAs and that may regulate RNA processing. In HeLa cells, the majority of GC-rich RNA binding proteins are associated with endogenous RNA transcripts. The separation of these proteins from endogenous RNA identified several proteins in addition to CUGBP1 that specifically interact with the GC-rich 5′ region of C/EBPβ mRNA. One of these proteins was purified to homogeneity and was identified as calreticulin (CRT). CRT is a multifunctional protein involved in several biological processes, including interaction with and regulation of rubella virus RNA processing. Our data demonstrate that both CUGBP1 and CRT interact with GCU repeats within myotonin protein kinase and with GCN repeats within C/EBPα and C/EBPβ mRNAs. GCN repeats within these mRNAs form stable SL structures. The interaction of CRT with SL structures of C/EBPβ and C/EBPα mRNAs leads to inhibition of translation of C/EBP proteins in vitro and in vivo. Deletions or mutations abolishing the formation of SL structures within C/EBPα and C/EBPβ mRNAs lead to a failure of CRT to inhibit translation of C/EBP proteins. CRT-dependent inhibition of C/EBPα is sufficient to block the growth-inhibitory activity of C/EBPα. This finding further defines the molecular mechanism for posttranscriptional regulation of the C/EBPα and C/EBPβ proteins.

scholarly journals Posttranscriptional Regulation and RNA Binding Proteins in Cancer Biology

2015 ◽  
Vol 2015 ◽  
pp. 1-2 ◽  
Author(s):  
Claudia Ghigna ◽  
Luca Cartegni ◽  
Peter Jordan ◽  
Maria Paola Paronetto
Keyword(s):  
Posttranscriptional Regulation ◽  
Cancer Biology ◽  
Binding Proteins ◽  
Rna Binding ◽  
Rna Binding Proteins
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