A photolyase-like protein from Agrobacterium tumefaciens with an iron-sulfur cluster.

Photolyases and cryptochromes are evolutionarily related flavoproteins with distinct functions. While photolyases can repair UV-induced DNA lesions in a light-dependent manner, cryptochromes regulate growth, development and the circadian clock in plants and animals. Here we report about two photolya...

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Autores principales:	Inga Oberpichler, Antonio J Pierik, Janine Wesslowski, Richard Pokorny, Ran Rosen, Michal Vugman, Fan Zhang, Olivia Neubauer, Eliora Z Ron, Alfred Batschauer, Tilman Lamparter
Formato:	article
Lenguaje:	EN
Publicado:	Public Library of Science (PLoS) 2011
Materias:	Medicine R Science Q
Acceso en línea:	https://doaj.org/article/aa5f6904bd55418a95f11cd5142fba09
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spelling	oai:doaj.org-article:aa5f6904bd55418a95f11cd5142fba092021-11-18T07:35:23ZA photolyase-like protein from Agrobacterium tumefaciens with an iron-sulfur cluster.1932-620310.1371/journal.pone.0026775https://doaj.org/article/aa5f6904bd55418a95f11cd5142fba092011-01-01T00:00:00Zhttps://www.ncbi.nlm.nih.gov/pmc/articles/pmid/22066008/?tool=EBIhttps://doaj.org/toc/1932-6203Photolyases and cryptochromes are evolutionarily related flavoproteins with distinct functions. While photolyases can repair UV-induced DNA lesions in a light-dependent manner, cryptochromes regulate growth, development and the circadian clock in plants and animals. Here we report about two photolyase-related proteins, named PhrA and PhrB, found in the phytopathogen Agrobacterium tumefaciens. PhrA belongs to the class III cyclobutane pyrimidine dimer (CPD) photolyases, the sister class of plant cryptochromes, while PhrB belongs to a new class represented in at least 350 bacterial organisms. Both proteins contain flavin adenine dinucleotide (FAD) as a primary catalytic cofactor, which is photoreduceable by blue light. Spectral analysis of PhrA confirmed the presence of 5,10-methenyltetrahydrofolate (MTHF) as antenna cofactor. PhrB comprises also an additional chromophore, absorbing in the short wavelength region but its spectrum is distinct from known antenna cofactors in other photolyases. Homology modeling suggests that PhrB contains an Fe-S cluster as cofactor which was confirmed by elemental analysis and EPR spectroscopy. According to protein sequence alignments the classical tryptophan photoreduction pathway is present in PhrA but absent in PhrB. Although PhrB is clearly distinguished from other photolyases including PhrA it is, like PhrA, required for in vivo photoreactivation. Moreover, PhrA can repair UV-induced DNA lesions in vitro. Thus, A. tumefaciens contains two photolyase homologs of which PhrB represents the first member of the cryptochrome/photolyase family (CPF) that contains an iron-sulfur cluster.Inga OberpichlerAntonio J PierikJanine WesslowskiRichard PokornyRan RosenMichal VugmanFan ZhangOlivia NeubauerEliora Z RonAlfred BatschauerTilman LamparterPublic Library of Science (PLoS)articleMedicineRScienceQENPLoS ONE, Vol 6, Iss 10, p e26775 (2011)
institution	DOAJ
collection	DOAJ
language	EN
topic	Medicine R Science Q
spellingShingle	Medicine R Science Q Inga Oberpichler Antonio J Pierik Janine Wesslowski Richard Pokorny Ran Rosen Michal Vugman Fan Zhang Olivia Neubauer Eliora Z Ron Alfred Batschauer Tilman Lamparter A photolyase-like protein from Agrobacterium tumefaciens with an iron-sulfur cluster.
description	Photolyases and cryptochromes are evolutionarily related flavoproteins with distinct functions. While photolyases can repair UV-induced DNA lesions in a light-dependent manner, cryptochromes regulate growth, development and the circadian clock in plants and animals. Here we report about two photolyase-related proteins, named PhrA and PhrB, found in the phytopathogen Agrobacterium tumefaciens. PhrA belongs to the class III cyclobutane pyrimidine dimer (CPD) photolyases, the sister class of plant cryptochromes, while PhrB belongs to a new class represented in at least 350 bacterial organisms. Both proteins contain flavin adenine dinucleotide (FAD) as a primary catalytic cofactor, which is photoreduceable by blue light. Spectral analysis of PhrA confirmed the presence of 5,10-methenyltetrahydrofolate (MTHF) as antenna cofactor. PhrB comprises also an additional chromophore, absorbing in the short wavelength region but its spectrum is distinct from known antenna cofactors in other photolyases. Homology modeling suggests that PhrB contains an Fe-S cluster as cofactor which was confirmed by elemental analysis and EPR spectroscopy. According to protein sequence alignments the classical tryptophan photoreduction pathway is present in PhrA but absent in PhrB. Although PhrB is clearly distinguished from other photolyases including PhrA it is, like PhrA, required for in vivo photoreactivation. Moreover, PhrA can repair UV-induced DNA lesions in vitro. Thus, A. tumefaciens contains two photolyase homologs of which PhrB represents the first member of the cryptochrome/photolyase family (CPF) that contains an iron-sulfur cluster.
format	article
author	Inga Oberpichler Antonio J Pierik Janine Wesslowski Richard Pokorny Ran Rosen Michal Vugman Fan Zhang Olivia Neubauer Eliora Z Ron Alfred Batschauer Tilman Lamparter
author_facet	Inga Oberpichler Antonio J Pierik Janine Wesslowski Richard Pokorny Ran Rosen Michal Vugman Fan Zhang Olivia Neubauer Eliora Z Ron Alfred Batschauer Tilman Lamparter
author_sort	Inga Oberpichler
title	A photolyase-like protein from Agrobacterium tumefaciens with an iron-sulfur cluster.
title_short	A photolyase-like protein from Agrobacterium tumefaciens with an iron-sulfur cluster.
title_full	A photolyase-like protein from Agrobacterium tumefaciens with an iron-sulfur cluster.
title_fullStr	A photolyase-like protein from Agrobacterium tumefaciens with an iron-sulfur cluster.
title_full_unstemmed	A photolyase-like protein from Agrobacterium tumefaciens with an iron-sulfur cluster.
title_sort	photolyase-like protein from agrobacterium tumefaciens with an iron-sulfur cluster.
publisher	Public Library of Science (PLoS)
publishDate	2011
url	https://doaj.org/article/aa5f6904bd55418a95f11cd5142fba09
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A photolyase-like protein from Agrobacterium tumefaciens with an iron-sulfur cluster.

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