Staufen1 reads out structure and sequence features in ARF1
dsRNA for target recognition

a 2019

Staufen1 reads out structure and sequence features in ARF1 dsRNA for target recognition

YADAV, Deepak Kumar, Dagmar ZIGÁČKOVÁ, Maria ZLOBINA, Tomáš KLUMPLER, Christelle BEAUMONT et. al.

Základní údaje

Originální název

Staufen1 reads out structure and sequence features in ARF1 dsRNA for target recognition

Autoři

YADAV, Deepak Kumar (356 Indie, domácí), Dagmar ZIGÁČKOVÁ (203 Česká republika, domácí), Maria ZLOBINA (643 Rusko, domácí), Tomáš KLUMPLER (203 Česká republika, domácí), Christelle BEAUMONT (250 Francie, domácí), Monika KUBÍČKOVÁ (203 Česká republika, domácí), Štěpánka VAŇÁČOVÁ (203 Česká republika, domácí) a Peter LUKAVSKY (40 Rakousko, garant, domácí)

Vydání

FEBS Congress 2019, 2019

Další údaje

Jazyk

angličtina

Typ výsledku

Konferenční abstrakt

Obor

10608 Biochemistry and molecular biology

Stát vydavatele

Spojené státy

Utajení

není předmětem státního či obchodního tajemství

Odkazy

URL

Impakt faktor

Impact factor: 2.231

Kód RIV

RIV/00216224:14740/19:00108212

Organizační jednotka

Středoevropský technologický institut

ISSN

UT WoS

000486972400099

Klíčová slova anglicky

Staufen1; ARF1 dsRNA

Štítky

rivok

Příznaky

Mezinárodní význam

Změněno: 30. 3. 2020 14:19, Mgr. Pavla Foltynová, Ph.D.

Anotace

V originále

Most posttranscriptional regulation of gene expression is based on RNA elements in mRNAs recognized by RNAbinding proteins (RBPs). Besides primary sequence elements, a second layer of information is embedded in 3’UTRs of mRNAs in the form of RNA structure. Doublestranded RBPs (dsRBPs) can bind structures in 3’UTRs and then exert their function based on dsRNA target recognition through a combination of structure and sequence. Staufen1 (STAU1) is a dsRBP involved in mRNA transport and localization, translational control and mRNA decay by a STAU1mediated mRNA decay (SMD) pathway. The STAU1 binding site (SBS) within human ADPribosylation factor1 (ARF1) 3’UTR is one such target and STAU1 binding to the SBS regulates ARF1 cytoplasmic mRNA levels by the SMD pathway. However, how STAU1 recognizes specific mRNA targets is still unknown. Our structure of the ARF1 SBS STAU1 complex uncovers target recognition by STAU1. STAU1 dsRNA binding domain (dsRBD) 4 interacts with two pyrimidines and one purine from the minor groove side via helix alfa1, beta1beta2 loop anchors the dsRBD at the end of the dsRNA and lysines in helix alfa2 bind to the phosphodiester backbone from the major groove side. STAU1 dsRBD3 displays the same binding mode with specific recognition of one guanine base. Mutants disrupting minor groove recognition of ARF1 SBS reduce SMD in vivo but have minor effect on in vitro binding. Our data suggest how dsRNA recognition by STAU1 mediates diverse functions in gene expression pathways.

Návaznosti

GA18-08153S, projekt VaV

Název: Molekulární podstata Staufen zprostředkované funkce 3'UTR

Investor: Grantová agentura ČR, Molecular basis of Staufen-mediated 3´UTR function

Citovat

YADAV, Deepak Kumar, Dagmar ZIGÁČKOVÁ, Maria ZLOBINA, Tomáš KLUMPLER, Christelle BEAUMONT, Monika KUBÍČKOVÁ, Štěpánka VAŇÁČOVÁ a Peter LUKAVSKY. Staufen1 reads out structure and sequence features in ARF1 dsRNA for target recognition. In FEBS Congress 2019. 2019. ISSN 2211-5463.

@proceedings{1640523,
   author = {Yadav, Deepak Kumar and Zigáčková, Dagmar and Zlobina, Maria and Klumpler, Tomáš and Beaumont, Christelle and Kubíčková, Monika and Vaňáčová, Štěpánka and Lukavsky, Peter},
   booktitle = {FEBS Congress 2019},
   keywords = {Staufen1; ARF1 dsRNA},
   language = {eng},
   title = {Staufen1 reads out structure and sequence features in ARF1 dsRNA for target recognition},
   url = {https://2019.febscongress.org/abstract_preview.aspx?idAbstractEnc=4424170094095093093091424170},
   year = {2019}
}

TY  - CONF
ID  - 1640523
AU  - Yadav, Deepak Kumar - Zigáčková, Dagmar - Zlobina, Maria - Klumpler, Tomáš - Beaumont, Christelle - Kubíčková, Monika - Vaňáčová, Štěpánka - Lukavsky, Peter
PY  - 2019
TI  - Staufen1 reads out structure and sequence features in ARF1 dsRNA for target recognition
KW  - Staufen1
KW  - ARF1 dsRNA
UR  - https://2019.febscongress.org/abstract_preview.aspx?idAbstractEnc=4424170094095093093091424170
N2  - Most posttranscriptional regulation of gene expression is based on RNA elements in mRNAs recognized by RNAbinding proteins (RBPs). Besides primary sequence elements, a second layer of information is embedded in 3’UTRs of mRNAs in the form of RNA structure. Doublestranded RBPs (dsRBPs) can bind structures in 3’UTRs and then exert their function based on dsRNA target recognition through a combination of structure and sequence. Staufen1 (STAU1) is a dsRBP involved in mRNA transport and localization, translational control and mRNA decay by a STAU1mediated mRNA decay (SMD) pathway. The STAU1 binding site (SBS) within human ADPribosylation factor1 (ARF1) 3’UTR is one such target and STAU1 binding to the SBS regulates ARF1 cytoplasmic mRNA levels by the SMD pathway. However, how STAU1 recognizes specific mRNA targets is still unknown. Our structure of the ARF1 SBS STAU1 complex uncovers target recognition by STAU1. STAU1 dsRNA binding domain (dsRBD) 4 interacts with two pyrimidines and one purine from the minor groove side via helix alfa1, beta1beta2 loop anchors the dsRBD at the end of the dsRNA and lysines in helix alfa2 bind to the phosphodiester backbone from the major groove side. STAU1 dsRBD3 displays the same binding mode with specific recognition of one guanine base. Mutants disrupting minor groove recognition of ARF1 SBS reduce SMD in vivo but have minor effect on in vitro binding. Our data suggest how dsRNA recognition by STAU1 mediates diverse functions in gene expression pathways.
ER  -

Podrobný výpis o publikaci