Translational initiation factors IF-1 and eIF-2α share an RNA-binding motif with prokaryotic ribosomal protein S1 and polynucleotide phosphorylase

Gene ◽  
1992 ◽  
Vol 119 (1) ◽  
pp. 107-111 ◽  
Author(s):  
Michael Gribskov
Keyword(s):  
Ribosomal Protein ◽  
Rna Binding ◽  
Binding Motif ◽  
Polynucleotide Phosphorylase ◽  
Translational Initiation ◽  
Initiation Factors ◽  
Ribosomal Protein S1

scholarly journals Translational induction of ATF4 during integrated stress response requires noncanonical initiation factors eIF2D and DENR

2020 ◽  
Vol 11 (1) ◽  
Author(s):  
Deepika Vasudevan ◽  
Sarah D. Neuman ◽  
Amy Yang ◽  
Lea Lough ◽  
Brian Brown ◽  
...  
Keyword(s):  
Stress Response ◽  
Er Stress ◽  
Stress Responses ◽  
Rna Binding ◽  
Open Reading Frames ◽  
Binding Motif ◽  
Integrated Stress Response ◽  
Developmental Defects ◽  
Initiation Factors

Abstract The Integrated Stress Response (ISR) helps metazoan cells adapt to cellular stress by limiting the availability of initiator methionyl-tRNA for translation. Such limiting conditions paradoxically stimulate the translation of ATF4 mRNA through a regulatory 5′ leader sequence with multiple upstream Open Reading Frames (uORFs), thereby activating stress-responsive gene expression. Here, we report the identification of two critical regulators of such ATF4 induction, the noncanonical initiation factors eIF2D and DENR. Loss of eIF2D and DENR in Drosophila results in increased vulnerability to amino acid deprivation, susceptibility to retinal degeneration caused by endoplasmic reticulum (ER) stress, and developmental defects similar to ATF4 mutants. eIF2D requires its RNA-binding motif for regulation of 5′ leader-mediated ATF4 translation. Consistently, eIF2D and DENR deficient human cells show impaired ATF4 protein induction in response to ER stress. Altogether, our findings indicate that eIF2D and DENR are critical mediators of ATF4 translational induction and stress responses in vivo.

scholarly journals Ribosomal protein L7a binds RNA through two distinct RNA-binding domains

2004 ◽  
Vol 385 (1) ◽  
pp. 289-299 ◽  
Author(s):  
Giulia RUSSO ◽  
Monica CUCCURESE ◽  
Gianluca MONTI ◽  
Annapina RUSSO ◽  
Angela AMORESANO ◽  
...  
Keyword(s):  
Ribosomal Protein ◽  
Rna Binding ◽  
Limited Proteolysis ◽  
Ribosomal Subunit ◽  
The Other ◽  
Protein Domain ◽  
Binding Motif ◽  
Nucleic Acid Binding ◽  
Binding Domains ◽  
Rna Binding Domains

The human ribosomal protein L7a is a component of the major ribosomal subunit. We previously identified three nuclear-localization-competent domains within L7a, and demonstrated that the domain defined by aa (amino acids) 52–100 is necessary, although not sufficient, to target the L7a protein to the nucleoli. We now demonstrate that L7a interacts in vitro with a presumably G-rich RNA structure, which has yet to be defined. We also demonstrate that the L7a protein contains two RNA-binding domains: one encompassing aa 52–100 (RNAB1) and the other encompassing aa 101–161 (RNAB2). RNAB1 does not contain any known nucleic-acid-binding motif, and may thus represent a new class of such motifs. On the other hand, a specific region of RNAB2 is highly conserved in several other protein components of the ribonucleoprotein complex. We have investigated the topology of the L7a–RNA complex using a recombinant form of the protein domain that encompasses residues 101–161 and a 30mer poly(G) oligonucleotide. Limited proteolysis and cross-linking experiments, and mass spectral analyses of the recombinant protein domain and its complex with poly(G) revealed the RNA-binding region.

scholarly journals The Contribution of Ribosomal Protein S1 to the Structure and Function of Qβ Replicase

Acta Naturae ◽  
2017 ◽  
Vol 9 (4) ◽  
pp. 26-30
Author(s):  
Z. Sh. Kutlubaeva ◽  
Е. V. Chetverina ◽  
A. B. Chetverin
Keyword(s):  
Crystal Structure ◽  
Ribosomal Protein ◽  
Rna Binding ◽  
Structure And Function ◽  
Ribosomal Protein S1 ◽  
Bacterial Ribosome ◽  
New Findings ◽  
Replicase Complex ◽  
And Function ◽  
Fixed Structure

The high resolution crystal structure of bacterial ribosome was determined more than 10 years ago; however, it contains no information on the structure of the largest ribosomal protein, S1. This unusual protein comprises six flexibly linked domains; therefore, it lacks a fixed structure and this prevents the formation of crystals. Besides being a component of the ribosome, protein S1 also serves as one of the four subunits of Q replicase, the RNA-directed RNA polymerase of bacteriophage Q. In each case, the role of this RNA-binding protein has been thought to consist in holding the template close to the active site of the enzyme. In recent years, a breakthrough was made in studies of protein S1 within Q replicase. This includes the discovery of its paradoxical ability to displace RNA from the replicase complex and determining the crystal structure of its fragment capable of performing this function. The new findings call for a re-examination of the contribution of protein S1 to the structure and function of the ribosome.

scholarly journals Ribosomal protein S7: a new RNA-binding motif with structural similarities to a DNA architectural factor

Structure ◽  
1997 ◽  
Vol 5 (9) ◽  
pp. 1199-1208 ◽  
Author(s):  
Harumi Hosaka ◽  
Atsushi Nakagawa ◽  
Isao Tanaka ◽  
Nao Harada ◽  
Kazunari Sano ◽  
...  
Keyword(s):  
Ribosomal Protein ◽  
Rna Binding ◽  
Binding Motif ◽  
Architectural Factor

scholarly journals Polynucleotide phosphorylase hinders mRNA degradation upon ribosomal protein S1 overexpression in Escherichia coli

RNA ◽  
2008 ◽  
Vol 14 (11) ◽  
pp. 2417-2429 ◽  
Author(s):  
F. Briani ◽  
S. Curti ◽  
F. Rossi ◽  
T. Carzaniga ◽  
P. Mauri ◽  
...  
Keyword(s):  
Escherichia Coli ◽  
Ribosomal Protein ◽  
Mrna Degradation ◽  
Polynucleotide Phosphorylase ◽  
Ribosomal Protein S1

Ribosomal protein S1 and initiation factor IF3 do not promote the ribosomal binding of ~ 19-nucleotide-long mDNA and mRNA models

1989 ◽  
Vol 67 (11-12) ◽  
pp. 812-817 ◽  
Author(s):  
Michael Laughrea ◽  
John Tam
Keyword(s):  
Ribosomal Protein ◽  
Initiation Site ◽  
Initiation Factor ◽  
Automated Synthesis ◽  
Main Function ◽  
Dna Templates ◽  
Initiation Factors ◽  
Synthetic Dna ◽  
Ribosomal Protein S1 ◽  
Direct Recognition

A number of model mDNAs and mRNAs, about 19 nucleotides in length, were obtained by automated synthesis and T7 RNA polymerase directed transcription from synthetic DNA templates, respectively. These mDNAs and mRNAs had Shine-Dalgarno sequences that were four to eight nucleotides long and their sequence was similar to the R17 coat protein initiation site. The effect of S1 or initiation factors (IFs) on the rate and extent of ribosomal binding of these mDNAs and mRNAs was investigated by nitrocellulose filtration. No effect was detected, suggesting that the main function of S1 or IFs included neither the direct recognition or binding of short messengers to the 30S subunits, nor their rejection as "false" for possessing the wrong sugars or an insufficient length. A pulse–chase experiment with one of the mRNAs also showed that S1 or IF3 did not influence the exchange rate of mRNA bound to the 30S subunit.Key words: ribosome, initiation, mRNA, ribosomal protein S1, initiation factor IF3.

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