Lichenicidin biosynthesis: LicP protease specificity
Autor(a) principal: | |
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Data de Publicação: | 2011 |
Tipo de documento: | Dissertação |
Idioma: | por |
Título da fonte: | Repositório Científico de Acesso Aberto de Portugal (Repositórios Cientìficos) |
Texto Completo: | http://hdl.handle.net/10773/7460 |
Resumo: | The lantibiotics are ribosomally synthesized peptides produced by Gram-positive cells that have antibiotic or morphogenic activity. After translation, the lantibiotics undergo chemical changes that result in the formation of unusual amino acids (lanthionine and methylanthionine), as well as the establishment of chemical bonds that confer a polycyclic structure to the peptide chain. After modifications occur, the leader sequence of the prelantibiotic is removed to yield the active lantibiotic, a process that may involve a single proteolitical reaction or two consecutive reactions. The lantibiotics are divided into classes according to their mechanism of biosynthesis and its biological activity. A particular sub-class of such compounds consists of two-component lantibiotics, in which each lantibiotic consists of two peptides, α and β, which act in synergy to confer it full activity. Lichenicidin is a two component lantibiotic produced by a microorganism commonly found in soil, Bacillus licheniformis. The leader sequence of one of the lichenicidin peptides (α-peptide) is totally removed through a single proteolytic reaction while the formation of the second peptide (β-peptide) implies the occurrence of two reactions of proteolysis, presumably made by the successive action of two enzymes, LicT and LicP, encoded in B. licheniformis genome. In this work, we evaluated the specificity of the LicP protease. For this purpose, we produced β-peptide mutants, in which some amino acids were replaced by Ala. The results indicated that LicP functionality is not impaired by single amino acid replacements. It was also shown that the Bliβ maturation process should, indeed, include the proteolysis of the leader sequence before the activity of LicP since an introduced mutation in the LicT cleavage site most probably inhibited the Bliβ full maturation. |
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Lichenicidin biosynthesis: LicP protease specificityMicrobiologiaAntibióticosProteasesPéptidosThe lantibiotics are ribosomally synthesized peptides produced by Gram-positive cells that have antibiotic or morphogenic activity. After translation, the lantibiotics undergo chemical changes that result in the formation of unusual amino acids (lanthionine and methylanthionine), as well as the establishment of chemical bonds that confer a polycyclic structure to the peptide chain. After modifications occur, the leader sequence of the prelantibiotic is removed to yield the active lantibiotic, a process that may involve a single proteolitical reaction or two consecutive reactions. The lantibiotics are divided into classes according to their mechanism of biosynthesis and its biological activity. A particular sub-class of such compounds consists of two-component lantibiotics, in which each lantibiotic consists of two peptides, α and β, which act in synergy to confer it full activity. Lichenicidin is a two component lantibiotic produced by a microorganism commonly found in soil, Bacillus licheniformis. The leader sequence of one of the lichenicidin peptides (α-peptide) is totally removed through a single proteolytic reaction while the formation of the second peptide (β-peptide) implies the occurrence of two reactions of proteolysis, presumably made by the successive action of two enzymes, LicT and LicP, encoded in B. licheniformis genome. In this work, we evaluated the specificity of the LicP protease. For this purpose, we produced β-peptide mutants, in which some amino acids were replaced by Ala. The results indicated that LicP functionality is not impaired by single amino acid replacements. It was also shown that the Bliβ maturation process should, indeed, include the proteolysis of the leader sequence before the activity of LicP since an introduced mutation in the LicT cleavage site most probably inhibited the Bliβ full maturation.Os lantibióticos são péptidos com actividade antibiótica ou morfogénica, sintetizados nos ribossomas de células Grampositivas. Após tradução, os lantibióticos sofrem modificações que resultam na formação de aminoácidos pouco comuns (lantionina e metil-lantionina) e na formação de ligações químicas que lhes conferem uma estrutura policíclica. Após estas modificações químicas, a sequência líder do pré-lantibiótico é removida tornando o péptido activo. Este processo pode envolver uma única reacção de proteólise ou duas reacções sucessivas. Os lantibióticos são divididos em diferentes classes consoante o seu mecanismo de biosíntese e a sua actividade biológica. Uma destas sub-classes inclui os lantibióticos de dois componentes, que são formados por dois péptidos, α e β, que, em conjunto, lhes conferem total actividade. A lichenicidina pertence a esta classe de lantibióticos. É produzida por Bacillus licheniformis, um microrganismo vulgarmente encontrado no solo. A remoção da sequência líder de um dos péptidos deste lantibiótico (péptido α) é removida numa única reacção proteolítica enquanto que, a formação do segundo péptido (o péptido β) implica a ocorrência de duas reacções de proteólise, presumivelmente efectuadas por acção sucessiva de duas enzimas, LicT e LicP, codificadas no genoma de B. licheniformis. Constituiu o objectivo do presente trabalho, avaliar a especificidade da protease LicP. Para tal, foram produzidos mutantes do péptido β nos quais, os aminoácidos da sequência líder foram substituídos por alanina. Os resultados mostraram que a funcionalidade da protease LicP não foi afectada pelas substituições de um único aminoácido. Os resultados mostraram, ainda, que a protease LicT deve actuar antes da protease LicP uma vez que, a introdução de uma mutação no local de corte da enzima LicT impediu a produção do péptido β.Universidade de Aveiro2013-11-27T08:46:03Z2011-09-16T00:00:00Z2011-09-16info:eu-repo/semantics/publishedVersioninfo:eu-repo/semantics/masterThesisapplication/pdfhttp://hdl.handle.net/10773/7460porFaria, Raquel Cristina Laranjeirainfo:eu-repo/semantics/openAccessreponame:Repositório Científico de Acesso Aberto de Portugal (Repositórios Cientìficos)instname:Agência para a Sociedade do Conhecimento (UMIC) - FCT - Sociedade da Informaçãoinstacron:RCAAP2024-02-22T11:12:57Zoai:ria.ua.pt:10773/7460Portal AgregadorONGhttps://www.rcaap.pt/oai/openaireopendoar:71602024-03-20T02:45:08.210080Repositório Científico de Acesso Aberto de Portugal (Repositórios Cientìficos) - Agência para a Sociedade do Conhecimento (UMIC) - FCT - Sociedade da Informaçãofalse |
dc.title.none.fl_str_mv |
Lichenicidin biosynthesis: LicP protease specificity |
title |
Lichenicidin biosynthesis: LicP protease specificity |
spellingShingle |
Lichenicidin biosynthesis: LicP protease specificity Faria, Raquel Cristina Laranjeira Microbiologia Antibióticos Proteases Péptidos |
title_short |
Lichenicidin biosynthesis: LicP protease specificity |
title_full |
Lichenicidin biosynthesis: LicP protease specificity |
title_fullStr |
Lichenicidin biosynthesis: LicP protease specificity |
title_full_unstemmed |
Lichenicidin biosynthesis: LicP protease specificity |
title_sort |
Lichenicidin biosynthesis: LicP protease specificity |
author |
Faria, Raquel Cristina Laranjeira |
author_facet |
Faria, Raquel Cristina Laranjeira |
author_role |
author |
dc.contributor.author.fl_str_mv |
Faria, Raquel Cristina Laranjeira |
dc.subject.por.fl_str_mv |
Microbiologia Antibióticos Proteases Péptidos |
topic |
Microbiologia Antibióticos Proteases Péptidos |
description |
The lantibiotics are ribosomally synthesized peptides produced by Gram-positive cells that have antibiotic or morphogenic activity. After translation, the lantibiotics undergo chemical changes that result in the formation of unusual amino acids (lanthionine and methylanthionine), as well as the establishment of chemical bonds that confer a polycyclic structure to the peptide chain. After modifications occur, the leader sequence of the prelantibiotic is removed to yield the active lantibiotic, a process that may involve a single proteolitical reaction or two consecutive reactions. The lantibiotics are divided into classes according to their mechanism of biosynthesis and its biological activity. A particular sub-class of such compounds consists of two-component lantibiotics, in which each lantibiotic consists of two peptides, α and β, which act in synergy to confer it full activity. Lichenicidin is a two component lantibiotic produced by a microorganism commonly found in soil, Bacillus licheniformis. The leader sequence of one of the lichenicidin peptides (α-peptide) is totally removed through a single proteolytic reaction while the formation of the second peptide (β-peptide) implies the occurrence of two reactions of proteolysis, presumably made by the successive action of two enzymes, LicT and LicP, encoded in B. licheniformis genome. In this work, we evaluated the specificity of the LicP protease. For this purpose, we produced β-peptide mutants, in which some amino acids were replaced by Ala. The results indicated that LicP functionality is not impaired by single amino acid replacements. It was also shown that the Bliβ maturation process should, indeed, include the proteolysis of the leader sequence before the activity of LicP since an introduced mutation in the LicT cleavage site most probably inhibited the Bliβ full maturation. |
publishDate |
2011 |
dc.date.none.fl_str_mv |
2011-09-16T00:00:00Z 2011-09-16 2013-11-27T08:46:03Z |
dc.type.status.fl_str_mv |
info:eu-repo/semantics/publishedVersion |
dc.type.driver.fl_str_mv |
info:eu-repo/semantics/masterThesis |
format |
masterThesis |
status_str |
publishedVersion |
dc.identifier.uri.fl_str_mv |
http://hdl.handle.net/10773/7460 |
url |
http://hdl.handle.net/10773/7460 |
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por |
language |
por |
dc.rights.driver.fl_str_mv |
info:eu-repo/semantics/openAccess |
eu_rights_str_mv |
openAccess |
dc.format.none.fl_str_mv |
application/pdf |
dc.publisher.none.fl_str_mv |
Universidade de Aveiro |
publisher.none.fl_str_mv |
Universidade de Aveiro |
dc.source.none.fl_str_mv |
reponame:Repositório Científico de Acesso Aberto de Portugal (Repositórios Cientìficos) instname:Agência para a Sociedade do Conhecimento (UMIC) - FCT - Sociedade da Informação instacron:RCAAP |
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Agência para a Sociedade do Conhecimento (UMIC) - FCT - Sociedade da Informação |
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RCAAP |
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RCAAP |
reponame_str |
Repositório Científico de Acesso Aberto de Portugal (Repositórios Cientìficos) |
collection |
Repositório Científico de Acesso Aberto de Portugal (Repositórios Cientìficos) |
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Repositório Científico de Acesso Aberto de Portugal (Repositórios Cientìficos) - Agência para a Sociedade do Conhecimento (UMIC) - FCT - Sociedade da Informação |
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1799137503686426624 |