2006
"Lock and key" recognition in the world of protein-RNA interactions: How ADAR2 binds RNA
ŠTEFL, RichardZákladní údaje
Originální název
"Lock and key" recognition in the world of protein-RNA interactions: How ADAR2 binds RNA
Název česky
"Lock and key" recognition in the world of protein-RNA interactions: How ADAR2 binds RNA
Autoři
ŠTEFL, Richard (203 Česká republika, garant)
Vydání
USA, xxx, 2006
Nakladatel
xxx
Další údaje
Jazyk
angličtina
Typ výsledku
Audiovizuální tvorba
Obor
10600 1.6 Biological sciences
Stát vydavatele
Spojené státy
Utajení
není předmětem státního či obchodního tajemství
Kód RIV
RIV/00216224:14310/06:00018577
Organizační jednotka
Přírodovědecká fakulta
Klíčová slova anglicky
NMR; protein-RNA interactions; gene regulation; structure
Štítky
Změněno: 22. 2. 2007 14:25, prof. Mgr. Richard Štefl, Ph.D.
V originále
The association of RNA-binding proteins with RNA transcript begins during transcription. Some of these early-binding proteins remain bound to RNA until it is degraded whereas others recognize and transiently bind to RNA during its maturation for specific processes such as splicing, processing, transport and localization. Some RNA-binding proteins function as RNA chaperones by helping the RNA, which is initially single-stranded, to form various secondary and tertiary structures. When folded these structured RNAs together with specific RNA sequences act as a signal for gene regulation. Adenosine deaminase that acts on RNA (ADAR) is a gene regulator that site-selectively modifies adenosines to inosines within RNA transcripts, thereby recoding genomic information. ADAR selects its substrate for deamination through recognition of certain double-helical irregularities within folded RNA transcript. This recognition is mediated using double-stranded RNA-binding motifs (dsRBMs) of ADAR. It will be demonstrated how ADAR dsRBMs bind a 71 nucleotide RNA encoding the R/G site of the glutamate-activated cation channel. We will show that each dsRBM binds a different structural element of the RNA substrate. ADAR dsRBM1 binds preferentially a stem capped by a pentaloop and ADAR dsRBM2 recognizes a stem containing two AC mismatches. Our structural and functional studies demonstrate that dsRBM, a motive known to bind any RNA duplexes with no sequence specificity, can preferentially bind certain RNA structures and thus mediates site-specific gene regulation.
Česky
The association of RNA-binding proteins with RNA transcript begins during transcription. Some of these early-binding proteins remain bound to RNA until it is degraded whereas others recognize and transiently bind to RNA during its maturation for specific processes such as splicing, processing, transport and localization. Some RNA-binding proteins function as RNA chaperones by helping the RNA, which is initially single-stranded, to form various secondary and tertiary structures. When folded these structured RNAs together with specific RNA sequences act as a signal for gene regulation. Adenosine deaminase that acts on RNA (ADAR) is a gene regulator that site-selectively modifies adenosines to inosines within RNA transcripts, thereby recoding genomic information. ADAR selects its substrate for deamination through recognition of certain double-helical irregularities within folded RNA transcript. This recognition is mediated using double-stranded RNA-binding motifs (dsRBMs) of ADAR. It will be demonstrated how ADAR dsRBMs bind a 71 nucleotide RNA encoding the R/G site of the glutamate-activated cation channel. We will show that each dsRBM binds a different structural element of the RNA substrate. ADAR dsRBM1 binds preferentially a stem capped by a pentaloop and ADAR dsRBM2 recognizes a stem containing two AC mismatches. Our structural and functional studies demonstrate that dsRBM, a motive known to bind any RNA duplexes with no sequence specificity, can preferentially bind certain RNA structures and thus mediates site-specific gene regulation.
Návaznosti
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