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

J 2020

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, garant, domácí) a Peter LUKAVSKY (40 Rakousko, domácí)

Vydání

Nucleic acids research, Oxford, Oxford University Press, 2020, 0305-1048

Další údaje

Jazyk

angličtina

Typ výsledku

Článek v odborném periodiku

Obor

10608 Biochemistry and molecular biology

Stát vydavatele

Velká Británie a Severní Irsko

Utajení

není předmětem státního či obchodního tajemství

Odkazy

URL

Impakt faktor

Impact factor: 16.971

Kód RIV

RIV/00216224:14740/20:00114622

Organizační jednotka

Středoevropský technologický institut

DOI

http://dx.doi.org/10.1093/nar/gkz1163

UT WoS

000525957000038

Klíčová slova anglicky

DOUBLE-STRANDED-RNA; NMR STRUCTURE DETERMINATION; LARGE-SCALE PREPARATION; BICOID MESSENGER-RNA; SECONDARY STRUCTURES; BINDING PROTEIN; DOMAIN; PURIFICATION; NOESY; LOCALIZATION

Štítky

CF BIC, rivok

Příznaky

Mezinárodní význam, Recenzováno

Změněno: 27. 10. 2024 15:12, Ing. Martina Blahová

Anotace

V originále

Staufen1 (STAU1) is a dsRNA binding protein mediating mRNA transport and localization, translational control and STAU1-mediated mRNA decay (SMD). The STAU1 binding site (SBS) within human ADP-ribosylation factorl (ARF1) 3'UTR binds STAU1 and this downregulates ARF1 cytoplasmic mRNA levels by SMD. However, how STAU1 recognizes specific mRNA targets is still under debate. 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 alpha 1, the beta 1-beta 2 loop anchors the dsRBD at the end of the dsRNA and lysines in helix alpha 2 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 affect in vitro binding and reduce SMD in vivo. Our data thus reveal how STAU1 recognizes minor groove features in dsRNA relevant for target selection.

Návaznosti

EE2.3.20.0042, projekt VaV

Název: Internacionalizace programu Strukturní biologie s důrazem na rozvoj nových směrů výzkumu

GA16-21341S, projekt VaV

Název: Studium úlohy uridylace RNA v lidských buňkách

Investor: Grantová agentura ČR, Studium úlohy uridylace RNA v lidských buňkách

GA18-08153S, projekt VaV

Název: Molekulární podstata Staufen zprostředkované funkce 3'UTR

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

LQ1601, projekt VaV

Název: CEITEC 2020 (Akronym: CEITEC2020)

Investor: Ministerstvo školství, mládeže a tělovýchovy ČR, CEITEC 2020

286154, interní kód MU

Název: SYLICA - Synergies of Life and Material Sciences to Create a New Future (Akronym: SYLICA)

Investor: Evropská unie, SYLICA - Synergies of Life and Material Sciences to Create a New Future, Kapacity

3014, interní kód MU

Název: Molecular basis of aberrant splicing of CFTR exon 9

Investor: EMBO (European Molecular Biology Organization), Molecular basis of aberrant splicing of CFTR exon 9

630758, interní kód MU

Název: Aberrant Splicing of CFTR Exon 9 (Akronym: ASCE)

Investor: Evropská unie, Aberrant Splicing of CFTR Exon 9, Lidé

90043, velká výzkumná infrastruktura

Název: CIISB

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. Nucleic acids research. Oxford: Oxford University Press, 2020, roč. 48, č. 4, s. 2091-2106. ISSN 0305-1048. Dostupné z: https://dx.doi.org/10.1093/nar/gkz1163.

@article{1720519,
   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},
   article_location = {Oxford},
   article_number = {4},
   doi = {http://dx.doi.org/10.1093/nar/gkz1163},
   keywords = {DOUBLE-STRANDED-RNA; NMR STRUCTURE DETERMINATION; LARGE-SCALE PREPARATION; BICOID MESSENGER-RNA; SECONDARY STRUCTURES; BINDING PROTEIN; DOMAIN; PURIFICATION; NOESY; LOCALIZATION},
   language = {eng},
   issn = {0305-1048},
   journal = {Nucleic acids research},
   title = {Staufen1 reads out structure and sequence features in ARF1 dsRNA for target recognition},
   url = {https://watermark.silverchair.com/gkz1163.pdf?token=AQECAHi208BE49Ooan9kkhW_Ercy7Dm3ZL_9Cf3qfKAc485ysgAAArMwggKvBgkqhkiG9w0BBwagggKgMIICnAIBADCCApUGCSqGSIb3DQEHATAeBglghkgBZQMEAS4wEQQM93m65EaHAul9lvZ3AgEQgIICZgl4kN1MOxCY84aEvwwQEi6vjxrtsNYzBuhYRTUjwbqxdd},
   volume = {48},
   year = {2020}
}

TY  - JOUR
ID  - 1720519
AU  - Yadav, Deepak Kumar - Zigáčková, Dagmar - Zlobina, Maria - Klumpler, Tomáš - Beaumont, Christelle - Kubíčková, Monika - Vaňáčová, Štěpánka - Lukavsky, Peter
PY  - 2020
TI  - Staufen1 reads out structure and sequence features in ARF1 dsRNA for target recognition
JF  - Nucleic acids research
VL  - 48
IS  - 4
SP  - 2091-2106
EP  - 2091-2106
PB  - Oxford University Press
SN  - 03051048
KW  - DOUBLE-STRANDED-RNA
KW  - NMR STRUCTURE DETERMINATION
KW  - LARGE-SCALE PREPARATION
KW  - BICOID MESSENGER-RNA
KW  - SECONDARY STRUCTURES
KW  - BINDING PROTEIN
KW  - DOMAIN
KW  - PURIFICATION
KW  - NOESY
KW  - LOCALIZATION
UR  - https://watermark.silverchair.com/gkz1163.pdf?token=AQECAHi208BE49Ooan9kkhW_Ercy7Dm3ZL_9Cf3qfKAc485ysgAAArMwggKvBgkqhkiG9w0BBwagggKgMIICnAIBADCCApUGCSqGSIb3DQEHATAeBglghkgBZQMEAS4wEQQM93m65EaHAul9lvZ3AgEQgIICZgl4kN1MOxCY84aEvwwQEi6vjxrtsNYzBuhYRTUjwbqxdd
L2  - https://watermark.silverchair.com/gkz1163.pdf?token=AQECAHi208BE49Ooan9kkhW_Ercy7Dm3ZL_9Cf3qfKAc485ysgAAArMwggKvBgkqhkiG9w0BBwagggKgMIICnAIBADCCApUGCSqGSIb3DQEHATAeBglghkgBZQMEAS4wEQQM93m65EaHAul9lvZ3AgEQgIICZgl4kN1MOxCY84aEvwwQEi6vjxrtsNYzBuhYRTUjwbqxdd
N2  - Staufen1 (STAU1) is a dsRNA binding protein mediating mRNA transport and localization, translational control and STAU1-mediated mRNA decay (SMD). The STAU1 binding site (SBS) within human ADP-ribosylation factorl (ARF1) 3'UTR binds STAU1 and this downregulates ARF1 cytoplasmic mRNA levels by SMD. However, how STAU1 recognizes specific mRNA targets is still under debate. 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 alpha 1, the beta 1-beta 2 loop anchors the dsRBD at the end of the dsRNA and lysines in helix alpha 2 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 affect in vitro binding and reduce SMD in vivo. Our data thus reveal how STAU1 recognizes minor groove features in dsRNA relevant for target selection.
ER  -

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. \textit{Nucleic acids research}. Oxford: Oxford University Press, 2020, roč.~48, č.~4, s.~2091-2106. ISSN~0305-1048. Dostupné z: https://dx.doi.org/10.1093/nar/gkz1163.

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