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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....
Autores principales: | , , , , |
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Formato: | Online Artículo Texto |
Lenguaje: | English |
Publicado: |
MDPI
2020
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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. |
format | Online Article Text |
id | pubmed-7345447 |
institution | National Center for Biotechnology Information |
language | English |
publishDate | 2020 |
publisher | MDPI |
record_format | MEDLINE/PubMed |
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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