The molecular dynamics study of the RNA-binding domain of ADAR2 bound to dsRNA

PASULKA, Josef, Jaroslav KOČA a Richard ŠTEFL. The molecular dynamics study of the RNA-binding domain of ADAR2 bound to dsRNA. In 7th Discussions in Structural Molecular Biology Nove Hrady, 12 - 14 March 2009. 2009. ISSN 1211-5894.

Základní údaje

• Originální název: The molecular dynamics study of the RNA-binding domain of ADAR2 bound to dsRNA
• Název česky: The molecular dynamics study of the RNA-binding domain of ADAR2 bound to dsRNA
• Autoři: PASULKA, Josef, Jaroslav KOČA a Richard ŠTEFL.
• Vydání: 7th Discussions in Structural Molecular Biology Nove Hrady, 12 - 14 March 2009, 2009.

Další údaje

• Originální jazyk: angličtina
• Typ výsledku: Konferenční abstrakt
• Obor: Genetika a molekulární biologie
• Stát vydavatele: Česká republika
• Utajení: není předmětem státního či obchodního tajemství
• Organizační jednotka: Přírodovědecká fakulta
• ISSN: 1211-5894
• Klíčová slova česky: molecular dynamics; RNA-binding motive; ADAR2; RNA recognition
• Klíčová slova anglicky: molecular dynamics; RNA-binding motive; ADAR2; RNA recognition

Anotace

Like RNA splicing, RNA editing alters the sequence of an RNA from that encoded in the DNA. Typically, a single RNA splicing reaction removes a large block of contiguous sequence, whereas each RNA editing reaction changes only one or two nucleotides. Therefore splicing is a cut-and-paste mechanism whereas editing is one of fine-tuning. RNA editing by adenosine deamination is catalyzed by members of an enzyme family known as adenosine deaminases that act on RNA (ADARs). ADARs are RNA editing enzymes that target double-stranded regions of nuclear-encoded RNA. ADARs are also interesting in regard to the remarkable double-stranded structures of their substrates and how enzyme specificity is achieved with little regard to sequence. ADARs from all organisms have a common domain structure that includes variable numbers of double-stranded RNA (dsRNA) binding motifs (dsRBMs) followed by a highly conserved C-terminal catalytic domain. We focused on the N-terminal non-catalytic domain ADAR2, which recognizes the dsRNA with A-C mismatches. Using MD simulations, we study the role of mismatches and their flexibility for the formation of dsRBM-RNA complexes.

Anotace česky

Like RNA splicing, RNA editing alters the sequence of an RNA from that encoded in the DNA. Typically, a single RNA splicing reaction removes a large block of contiguous sequence, whereas each RNA editing reaction changes only one or two nucleotides. Therefore splicing is a cut-and-paste mechanism whereas editing is one of fine-tuning. RNA editing by adenosine deamination is catalyzed by members of an enzyme family known as adenosine deaminases that act on RNA (ADARs). ADARs are RNA editing enzymes that target double-stranded regions of nuclear-encoded RNA. ADARs are also interesting in regard to the remarkable double-stranded structures of their substrates and how enzyme specificity is achieved with little regard to sequence. ADARs from all organisms have a common domain structure that includes variable numbers of double-stranded RNA (dsRNA) binding motifs (dsRBMs) followed by a highly conserved C-terminal catalytic domain. We focused on the N-terminal non-catalytic domain ADAR2, which recognizes the dsRNA with A-C mismatches. Using MD simulations, we study the role of mismatches and their flexibility for the formation of dsRBM-RNA complexes.

Návaznosti

• GA204/08/1212, projekt VaV: Název: Strukturní studium interakcí mezi proteiny a RNA účastnící se v mechanismu kontroly kvality RNA

Investor: Grantová agentura ČR, Strukturní studium interakcí mezi proteiny a RNA účastnící se v mechanismu kontroly kvality RNA

• IAA401630903, projekt VaV: Název: Strukturní podstata mechanismu ukončení transkripce nepolyadenylovaných transkriptů

Investor: Akademie věd ČR, Strukturní podstata mechanismu ukončení transkripce nepolyadenylovaných transkriptů

• LA08008, projekt VaV: Název: Strukturní studium interakcí mezi bíkovinami a poškozenou RNA.

Investor: Ministerstvo školství, mládeže a tělovýchovy ČR, Strukturní studium interakcí mezi bílkovinami a poškozenou RNA

• MSM0021622413, záměr: Název: Proteiny v metabolismu a při interakci organismů s prostředím

Investor: Ministerstvo školství, mládeže a tělovýchovy ČR, Proteiny v metabolismu a při interakci organismů s prostředím