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Studies on the Properties of the Sporulation Specific Protein Dit1 and Its Product Formyl Tyrosine

The dityrosine layer is a unique structure present in the spore wall of the budding yeast Saccharomyces cerevisiae. The primary constituent of this layer is bisformyl dityrosine. A sporulation-specific protein, Dit1 is localized in the spore cytosol and produces a precursor of bisformyl dityrosine....

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Autores principales: Basiony, Mostafa, Yang, Yan, Liu, Guoyu, Gao, Xiao-Dong, Nakanishi, Hideki
Formato: Online Artículo Texto
Lenguaje:English
Publicado: MDPI 2020
Materias:
Acceso en línea:https://www.ncbi.nlm.nih.gov/pmc/articles/PMC7345447/
https://www.ncbi.nlm.nih.gov/pubmed/32503197
http://dx.doi.org/10.3390/jof6020077
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author Basiony, Mostafa
Yang, Yan
Liu, Guoyu
Gao, Xiao-Dong
Nakanishi, Hideki
author_facet Basiony, Mostafa
Yang, Yan
Liu, Guoyu
Gao, Xiao-Dong
Nakanishi, Hideki
author_sort Basiony, Mostafa
collection PubMed
description The dityrosine layer is a unique structure present in the spore wall of the budding yeast Saccharomyces cerevisiae. The primary constituent of this layer is bisformyl dityrosine. A sporulation-specific protein, Dit1 is localized in the spore cytosol and produces a precursor of bisformyl dityrosine. Although Dit1 is similar to isocyanide synthases, the loss of Dit1 is not rescued by heterologous expression of the Pseudomonas aeruginosa isocyanide synthase, PvcA, indicating that Dit1 does not mediate isocyanidation. The product of Dit1 is most likely formyl tyrosine. Dit1 can produce its product when it is expressed in vegetative cells; however, formyl tyrosine was not detected in the crude cell lysate. We reasoned that formyl tyrosine is unstable and reacts with some molecule to form formyl tyrosine-containing molecules in the cell lysate. In support of this hypothesis, formyl tyrosine was detected when the lysate was hydrolyzed with a mild acid. The same property was also found for bisformyl dityrosine. Bisformyl dityrosine molecules assemble to form the dityrosine layer by an unknown mechanism. Given that bisformyl dityrosine can be released from the spore wall by mild hydrolysis, the process of formyl tyrosine-containing molecule formation may resemble the assembly of the dityrosine layer.
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spelling pubmed-73454472020-07-09 Studies on the Properties of the Sporulation Specific Protein Dit1 and Its Product Formyl Tyrosine Basiony, Mostafa Yang, Yan Liu, Guoyu Gao, Xiao-Dong Nakanishi, Hideki J Fungi (Basel) Article The dityrosine layer is a unique structure present in the spore wall of the budding yeast Saccharomyces cerevisiae. The primary constituent of this layer is bisformyl dityrosine. A sporulation-specific protein, Dit1 is localized in the spore cytosol and produces a precursor of bisformyl dityrosine. Although Dit1 is similar to isocyanide synthases, the loss of Dit1 is not rescued by heterologous expression of the Pseudomonas aeruginosa isocyanide synthase, PvcA, indicating that Dit1 does not mediate isocyanidation. The product of Dit1 is most likely formyl tyrosine. Dit1 can produce its product when it is expressed in vegetative cells; however, formyl tyrosine was not detected in the crude cell lysate. We reasoned that formyl tyrosine is unstable and reacts with some molecule to form formyl tyrosine-containing molecules in the cell lysate. In support of this hypothesis, formyl tyrosine was detected when the lysate was hydrolyzed with a mild acid. The same property was also found for bisformyl dityrosine. Bisformyl dityrosine molecules assemble to form the dityrosine layer by an unknown mechanism. Given that bisformyl dityrosine can be released from the spore wall by mild hydrolysis, the process of formyl tyrosine-containing molecule formation may resemble the assembly of the dityrosine layer. MDPI 2020-06-03 /pmc/articles/PMC7345447/ /pubmed/32503197 http://dx.doi.org/10.3390/jof6020077 Text en © 2020 by the authors. Licensee MDPI, Basel, Switzerland. This article is an open access article distributed under the terms and conditions of the Creative Commons Attribution (CC BY) license (http://creativecommons.org/licenses/by/4.0/).
spellingShingle Article
Basiony, Mostafa
Yang, Yan
Liu, Guoyu
Gao, Xiao-Dong
Nakanishi, Hideki
Studies on the Properties of the Sporulation Specific Protein Dit1 and Its Product Formyl Tyrosine
title Studies on the Properties of the Sporulation Specific Protein Dit1 and Its Product Formyl Tyrosine
title_full Studies on the Properties of the Sporulation Specific Protein Dit1 and Its Product Formyl Tyrosine
title_fullStr Studies on the Properties of the Sporulation Specific Protein Dit1 and Its Product Formyl Tyrosine
title_full_unstemmed Studies on the Properties of the Sporulation Specific Protein Dit1 and Its Product Formyl Tyrosine
title_short Studies on the Properties of the Sporulation Specific Protein Dit1 and Its Product Formyl Tyrosine
title_sort studies on the properties of the sporulation specific protein dit1 and its product formyl tyrosine
topic Article
url https://www.ncbi.nlm.nih.gov/pmc/articles/PMC7345447/
https://www.ncbi.nlm.nih.gov/pubmed/32503197
http://dx.doi.org/10.3390/jof6020077
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