Critical Reviews and Perspectives beta-CASP proteins removing RNA polymerase from DNA: when a torpedo is needed to shoot a sitting duck
Identifikátory výsledku
Kód výsledku v IS VaVaI
<a href="https://www.isvavai.cz/riv?ss=detail&h=RIV%2F61388971%3A_____%2F21%3A00549270" target="_blank" >RIV/61388971:_____/21:00549270 - isvavai.cz</a>
Výsledek na webu
<a href="https://academic.oup.com/nar/article/49/18/10221/6374178" target="_blank" >https://academic.oup.com/nar/article/49/18/10221/6374178</a>
DOI - Digital Object Identifier
<a href="http://dx.doi.org/10.1093/nar/gkab803" target="_blank" >10.1093/nar/gkab803</a>
Alternativní jazyky
Jazyk výsledku
angličtina
Název v původním jazyce
Critical Reviews and Perspectives beta-CASP proteins removing RNA polymerase from DNA: when a torpedo is needed to shoot a sitting duck
Popis výsledku v původním jazyce
During the first step of gene expression, RNA polymerase (RNAP) engages DNA to transcribe RNA, forming highly stable complexes. These complexes need to be dissociated at the end of transcription units or when RNAP stalls during elongation and becomes an obstacle ('sitting duck') to further transcription or replication. In this review, we first outline the mechanisms involved in these processes. Then, we explore in detail the torpedo mechanism whereby a 5'-3' RNA exonuclease (torpedo) latches itself onto the 5' end of RNA protruding from RNAP, degrades it and upon contact with RNAP, induces dissociation of the complex. This mechanism, originally described in Eukaryotes and executed by Xrn-type 5'-3' exonucleases, was recently found in Bacteria and Archaea, mediated by beta-CASP family exonucleases. We discuss the mechanistic aspects of this process across the three kingdoms of life and conclude that 5'-3' exoribonucleases (beta-CASP and Xrn families) involved in the ancient torpedo mechanism have emerged at least twice during evolution.
Název v anglickém jazyce
Critical Reviews and Perspectives beta-CASP proteins removing RNA polymerase from DNA: when a torpedo is needed to shoot a sitting duck
Popis výsledku anglicky
During the first step of gene expression, RNA polymerase (RNAP) engages DNA to transcribe RNA, forming highly stable complexes. These complexes need to be dissociated at the end of transcription units or when RNAP stalls during elongation and becomes an obstacle ('sitting duck') to further transcription or replication. In this review, we first outline the mechanisms involved in these processes. Then, we explore in detail the torpedo mechanism whereby a 5'-3' RNA exonuclease (torpedo) latches itself onto the 5' end of RNA protruding from RNAP, degrades it and upon contact with RNAP, induces dissociation of the complex. This mechanism, originally described in Eukaryotes and executed by Xrn-type 5'-3' exonucleases, was recently found in Bacteria and Archaea, mediated by beta-CASP family exonucleases. We discuss the mechanistic aspects of this process across the three kingdoms of life and conclude that 5'-3' exoribonucleases (beta-CASP and Xrn families) involved in the ancient torpedo mechanism have emerged at least twice during evolution.
Klasifikace
Druh
J<sub>imp</sub> - Článek v periodiku v databázi Web of Science
CEP obor
—
OECD FORD obor
10608 - Biochemistry and molecular biology
Návaznosti výsledku
Projekt
<a href="/cs/project/GA19-12956S" target="_blank" >GA19-12956S: Klíčové aspekty mykobakteriální transkriprce: SigA, podjednotka RNAP rozpoznávající promotor a její nově identifikovaný vazebný partner.</a><br>
Návaznosti
P - Projekt vyzkumu a vyvoje financovany z verejnych zdroju (s odkazem do CEP)
Ostatní
Rok uplatnění
2021
Kód důvěrnosti údajů
S - Úplné a pravdivé údaje o projektu nepodléhají ochraně podle zvláštních právních předpisů
Údaje specifické pro druh výsledku
Název periodika
Nucleic Acids Research
ISSN
0305-1048
e-ISSN
1362-4962
Svazek periodika
49
Číslo periodika v rámci svazku
18
Stát vydavatele periodika
GB - Spojené království Velké Británie a Severního Irska
Počet stran výsledku
14
Strana od-do
10221-10234
Kód UT WoS článku
000715870700008
EID výsledku v databázi Scopus
2-s2.0-85118286382