External guide sequence technology: A path to development of novel antimicrobial therapeutics
RNase P is a ribozyme originally identified for its role in maturation of tRNAs by cleavage of precursor tRNAs (pre-tRNAs) at the 5′-end termini. RNase P is a ribonucleoprotein consisting of a catalytic RNA molecule and, depending on the organism, one or more cofactor proteins. The site of cleavage...
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paper:paper_00778923_v1354_n1_p98_DaviesSala2023-06-08T15:07:31Z External guide sequence technology: A path to development of novel antimicrobial therapeutics Davies Sala, Carol G. Soler Bistué, Alfonso Juan de la Cruz Zorreguieta, Angeles Tolmasky, Marcelo Eduardo Antimicrobials Antisense Drug design External guide sequence RNase P aminoglycoside 6' n acetyltransferase type Ib antibiotic agent bacterial enzyme FtsZ protein messenger RNA ribonuclease P unclassified drug antiinfective agent antisense oligonucleotide bacterial RNA ribozyme antibiotic resistance Article bacterial infection Brucella melitensis Cytomegalovirus enzyme inhibition Escherichia coli external guide sequence Francisella tularensis gene expression genetic procedures Hepatitis B virus human Human immunodeficiency virus Influenza virus nonhuman protein cleavage protein targeting Salmonella enterica serovar Typhimurium virus virus infection Yersinia pestis Bacterial Infections bacterium biological model chemistry conformation drug effects genetics metabolism microbiology Anti-Bacterial Agents Bacteria Bacterial Infections Humans Models, Genetic Nucleic Acid Conformation Oligoribonucleotides, Antisense Ribonuclease P RNA, Bacterial RNA, Catalytic RNase P is a ribozyme originally identified for its role in maturation of tRNAs by cleavage of precursor tRNAs (pre-tRNAs) at the 5′-end termini. RNase P is a ribonucleoprotein consisting of a catalytic RNA molecule and, depending on the organism, one or more cofactor proteins. The site of cleavage of a pre-tRNA is identified by its tertiary structure; and any RNA molecule can be cleaved by RNase P as long as the RNA forms a duplex that resembles the regional structure in the pre-tRNA. When the antisense sequence that forms the duplex with the strand that is subsequently cleaved by RNase P is in a separate molecule, it is called an external guide sequence (EGS). These fundamental observations are the basis for EGS technology, which consists of inhibiting gene expression by utilizing an EGS that elicits RNase P-mediated cleavage of a target mRNA molecule. EGS technology has been used to inhibit expression of a wide variety of genes, and may help development of novel treatments of diseases, including multidrug-resistant bacterial and viral infections. © 2015 The New York Academy of Sciences. Fil:Davies-Sala, C. Universidad de Buenos Aires. Facultad de Ciencias Exactas y Naturales; Argentina. Fil:Soler-Bistué, A. Universidad de Buenos Aires. Facultad de Ciencias Exactas y Naturales; Argentina. Fil:Zorreguieta, A. Universidad de Buenos Aires. Facultad de Ciencias Exactas y Naturales; Argentina. Fil:Tolmasky, M.E. Universidad de Buenos Aires. Facultad de Ciencias Exactas y Naturales; Argentina. 2015 https://bibliotecadigital.exactas.uba.ar/collection/paper/document/paper_00778923_v1354_n1_p98_DaviesSala http://hdl.handle.net/20.500.12110/paper_00778923_v1354_n1_p98_DaviesSala |
institution |
Universidad de Buenos Aires |
institution_str |
I-28 |
repository_str |
R-134 |
collection |
Biblioteca Digital - Facultad de Ciencias Exactas y Naturales (UBA) |
topic |
Antimicrobials Antisense Drug design External guide sequence RNase P aminoglycoside 6' n acetyltransferase type Ib antibiotic agent bacterial enzyme FtsZ protein messenger RNA ribonuclease P unclassified drug antiinfective agent antisense oligonucleotide bacterial RNA ribozyme antibiotic resistance Article bacterial infection Brucella melitensis Cytomegalovirus enzyme inhibition Escherichia coli external guide sequence Francisella tularensis gene expression genetic procedures Hepatitis B virus human Human immunodeficiency virus Influenza virus nonhuman protein cleavage protein targeting Salmonella enterica serovar Typhimurium virus virus infection Yersinia pestis Bacterial Infections bacterium biological model chemistry conformation drug effects genetics metabolism microbiology Anti-Bacterial Agents Bacteria Bacterial Infections Humans Models, Genetic Nucleic Acid Conformation Oligoribonucleotides, Antisense Ribonuclease P RNA, Bacterial RNA, Catalytic |
spellingShingle |
Antimicrobials Antisense Drug design External guide sequence RNase P aminoglycoside 6' n acetyltransferase type Ib antibiotic agent bacterial enzyme FtsZ protein messenger RNA ribonuclease P unclassified drug antiinfective agent antisense oligonucleotide bacterial RNA ribozyme antibiotic resistance Article bacterial infection Brucella melitensis Cytomegalovirus enzyme inhibition Escherichia coli external guide sequence Francisella tularensis gene expression genetic procedures Hepatitis B virus human Human immunodeficiency virus Influenza virus nonhuman protein cleavage protein targeting Salmonella enterica serovar Typhimurium virus virus infection Yersinia pestis Bacterial Infections bacterium biological model chemistry conformation drug effects genetics metabolism microbiology Anti-Bacterial Agents Bacteria Bacterial Infections Humans Models, Genetic Nucleic Acid Conformation Oligoribonucleotides, Antisense Ribonuclease P RNA, Bacterial RNA, Catalytic Davies Sala, Carol G. Soler Bistué, Alfonso Juan de la Cruz Zorreguieta, Angeles Tolmasky, Marcelo Eduardo External guide sequence technology: A path to development of novel antimicrobial therapeutics |
topic_facet |
Antimicrobials Antisense Drug design External guide sequence RNase P aminoglycoside 6' n acetyltransferase type Ib antibiotic agent bacterial enzyme FtsZ protein messenger RNA ribonuclease P unclassified drug antiinfective agent antisense oligonucleotide bacterial RNA ribozyme antibiotic resistance Article bacterial infection Brucella melitensis Cytomegalovirus enzyme inhibition Escherichia coli external guide sequence Francisella tularensis gene expression genetic procedures Hepatitis B virus human Human immunodeficiency virus Influenza virus nonhuman protein cleavage protein targeting Salmonella enterica serovar Typhimurium virus virus infection Yersinia pestis Bacterial Infections bacterium biological model chemistry conformation drug effects genetics metabolism microbiology Anti-Bacterial Agents Bacteria Bacterial Infections Humans Models, Genetic Nucleic Acid Conformation Oligoribonucleotides, Antisense Ribonuclease P RNA, Bacterial RNA, Catalytic |
description |
RNase P is a ribozyme originally identified for its role in maturation of tRNAs by cleavage of precursor tRNAs (pre-tRNAs) at the 5′-end termini. RNase P is a ribonucleoprotein consisting of a catalytic RNA molecule and, depending on the organism, one or more cofactor proteins. The site of cleavage of a pre-tRNA is identified by its tertiary structure; and any RNA molecule can be cleaved by RNase P as long as the RNA forms a duplex that resembles the regional structure in the pre-tRNA. When the antisense sequence that forms the duplex with the strand that is subsequently cleaved by RNase P is in a separate molecule, it is called an external guide sequence (EGS). These fundamental observations are the basis for EGS technology, which consists of inhibiting gene expression by utilizing an EGS that elicits RNase P-mediated cleavage of a target mRNA molecule. EGS technology has been used to inhibit expression of a wide variety of genes, and may help development of novel treatments of diseases, including multidrug-resistant bacterial and viral infections. © 2015 The New York Academy of Sciences. |
author |
Davies Sala, Carol G. Soler Bistué, Alfonso Juan de la Cruz Zorreguieta, Angeles Tolmasky, Marcelo Eduardo |
author_facet |
Davies Sala, Carol G. Soler Bistué, Alfonso Juan de la Cruz Zorreguieta, Angeles Tolmasky, Marcelo Eduardo |
author_sort |
Davies Sala, Carol G. |
title |
External guide sequence technology: A path to development of novel antimicrobial therapeutics |
title_short |
External guide sequence technology: A path to development of novel antimicrobial therapeutics |
title_full |
External guide sequence technology: A path to development of novel antimicrobial therapeutics |
title_fullStr |
External guide sequence technology: A path to development of novel antimicrobial therapeutics |
title_full_unstemmed |
External guide sequence technology: A path to development of novel antimicrobial therapeutics |
title_sort |
external guide sequence technology: a path to development of novel antimicrobial therapeutics |
publishDate |
2015 |
url |
https://bibliotecadigital.exactas.uba.ar/collection/paper/document/paper_00778923_v1354_n1_p98_DaviesSala http://hdl.handle.net/20.500.12110/paper_00778923_v1354_n1_p98_DaviesSala |
work_keys_str_mv |
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