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Substrate profiling of human transglutaminase 1 using cDNA display and next-generation sequencing.
Munaweera, T I K; Damnjanovic, Jasmina; Camagna, Maurizio; Nezu, Moeri; Jia, Beixi; Hitomi, Kiyotaka; Nemoto, Naoto; Nakano, Hideo.
Afiliación
  • Munaweera TIK; Laboratory of Molecular Biotechnology, Graduate School of Bioagricultural Sciences, Nagoya University, Nagoya, Japan.
  • Damnjanovic J; Laboratory of Molecular Biotechnology, Graduate School of Bioagricultural Sciences, Nagoya University, Nagoya, Japan.
  • Camagna M; Laboratory of Plant Pathology, Graduate School of Bioagricultural Sciences, Nagoya University, Nagoya, Japan.
  • Nezu M; Laboratory of Molecular Biotechnology, Graduate School of Bioagricultural Sciences, Nagoya University, Nagoya, Japan.
  • Jia B; Laboratory of Molecular Biotechnology, Graduate School of Bioagricultural Sciences, Nagoya University, Nagoya, Japan.
  • Hitomi K; Laboratory of Cellular Biochemistry, Graduate School of Pharmaceutical Sciences, Nagoya University, Nagoya, Japan.
  • Nemoto N; Laboratory of Evolutionary Molecular Engineering, Graduate School of Science and Engineering, Saitama University , Saitama, Japan.
  • Nakano H; Laboratory of Molecular Biotechnology, Graduate School of Bioagricultural Sciences, Nagoya University, Nagoya, Japan.
Biosci Biotechnol Biochem ; 88(6): 620-629, 2024 May 22.
Article en En | MEDLINE | ID: mdl-38479783
ABSTRACT
Human transglutaminase 1 (TG1) modulates skin development, while its involvement in diseases remains poorly understood, necessitating comprehensive exploration of its substrate interactions. To study the substrate profile of TG1, an in vitro selection system based on cDNA display technology was used to screen two peptide libraries with mutations at varying distance from the reactive glutamine. Next-generation sequencing and bioinformatics analysis of the selected DNA pools revealed a detailed TG1 substrate profile, indicating preferred and non-preferred amino acid sequences. The peptide sequence, AEQHKLPSKWPF, was identified showing high reactivity and specificity to TG1. The position weight matrix calculated from the per amino acid enrichment factors was employed to search human proteins using an in-house algorithm, revealing six known TG1 substrate proteins with high scores, alongside a list of candidate substrates currently under investigation. Our findings are expected to assist in future medical diagnoses and development of treatments for skin disorders.
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Texto completo: 1 Colección: 01-internacional Base de datos: MEDLINE Asunto principal: Transglutaminasas / ADN Complementario / Secuenciación de Nucleótidos de Alto Rendimiento Límite: Humans Idioma: En Revista: Biosci Biotechnol Biochem Asunto de la revista: BIOQUIMICA / BIOTECNOLOGIA Año: 2024 Tipo del documento: Article País de afiliación: Japón Pais de publicación: Reino Unido
Texto completo
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Texto completo: 1 Colección: 01-internacional Base de datos: MEDLINE Asunto principal: Transglutaminasas / ADN Complementario / Secuenciación de Nucleótidos de Alto Rendimiento Límite: Humans Idioma: En Revista: Biosci Biotechnol Biochem Asunto de la revista: BIOQUIMICA / BIOTECNOLOGIA Año: 2024 Tipo del documento: Article País de afiliación: Japón Pais de publicación: Reino Unido