Your browser doesn't support javascript.
loading
Abundant Perithecial Protein (APP) from Neurospora is a primitive functional analog of ocular crystallins.
Pawar, Asmita D; Kiran, Uday; Raman, Rajeev; Chandani, Sushil; Sharma, Yogendra.
Afiliação
  • Pawar AD; CSIR-Centre for Cellular and Molecular Biology (CCMB), Uppal Road, Hyderabad, 500 007, India.
  • Kiran U; CSIR-Centre for Cellular and Molecular Biology (CCMB), Uppal Road, Hyderabad, 500 007, India; Academy of Scientific and Innovative Research (AcSIR), Ghaziabad, India.
  • Raman R; CSIR-Centre for Cellular and Molecular Biology (CCMB), Uppal Road, Hyderabad, 500 007, India.
  • Chandani S; 13, Plot 32, LIC Colony, W Marredpally, Secunderabad, 500026, Telangana, India.
  • Sharma Y; CSIR-Centre for Cellular and Molecular Biology (CCMB), Uppal Road, Hyderabad, 500 007, India; Academy of Scientific and Innovative Research (AcSIR), Ghaziabad, India; Indian Institute of Science Education and Research (IISER), Berhampur, Orissa, India. Electronic address: yogendra@ccmb.res.in.
Biochem Biophys Res Commun ; 516(3): 796-800, 2019 08 27.
Article em En | MEDLINE | ID: mdl-31255285
The eye arose during the Cambrian explosion from pre-existing proteins that would have been recruited for the formation of the specialized components of this organ, such as the transparent lens. Proteins suitable for the role of lens crystallins would need to possess unusual physical properties and the study of such earliest analogs of ocular crystallins would add to our understanding of the nature of recruitment of proteins as lens/corneal crystallins. We show that the Abundant Perithecial Protein (APP) of the fungi Neurospora and Sordaria fulfils the criteria for an early crystallin analog. The perithecia in these fungal species are phototropic, and APP accumulates at a high concentration in the neck of the pitcher-shaped perithecium. Spores are formed at the base of the perithecium, and light contributes to their maturation. The hydrodynamic properties of APP appear to exclude dimer formation or aggregation at high protein concentrations. APP is also deficient in Ca2+ binding, a property seen in its close homolog, the calcium-binding cell adhesion molecule (DdCAD-1) from Dictyostelium discoidum. Comparable to crystallins, APP occurs in high concentrations and seems to have dispensed with Ca2+ binding in exchange for greater stability. These crystallin-like attributes of APP lead us to demonstrate that it is a primitive form of ocular crystallins.
Assuntos
Palavras-chave

Texto completo: 1 Coleções: 01-internacional Base de dados: MEDLINE Assunto principal: Esporos Fúngicos / Proteínas de Ligação ao Cálcio / Proteínas Fúngicas / Cristalinas / Neurospora Tipo de estudo: Prognostic_studies Idioma: En Ano de publicação: 2019 Tipo de documento: Article

Texto completo: 1 Coleções: 01-internacional Base de dados: MEDLINE Assunto principal: Esporos Fúngicos / Proteínas de Ligação ao Cálcio / Proteínas Fúngicas / Cristalinas / Neurospora Tipo de estudo: Prognostic_studies Idioma: En Ano de publicação: 2019 Tipo de documento: Article