Abstract
Sex differentiation is a complex process where sexually indifferent embryo progressively acquires male or female characteristics via tightly controlled, perfectly timed, and sophisticatedly intertwined chain of events. This process is controlled and regulated by a set of specific proteins, with one of the first steps in sex differentiation being the activation of the Y-chromosomal Sry gene (sexdetermining region Y) in males that acts as a switch from undifferentiated gonad somatic cells to testis development. There are several key players in this process, which constitute the Sry transcriptional network, and collective action of which governs testis determination. Although it is accepted now that many proteins engaged in signal transduction as well as regulation and control of various biological processes are intrinsically disordered (i.e., do not have unique structure and remain unstructured, or incompletely structured, under physiological conditions), the roles and profusion of intrinsic disorder in proteins involved in the male sex determination have not been accessed as of yet. The goal of this study is to cover this gap by analyzing some key players of the Sry transcriptional network. To this end, we employed a broad set of computational tools for intrinsic disorder analysis and conducted intensive literature search in order to gain information on the structural peculiarities of the Sry networkrelated proteins, their intrinsic disorder predispositions, and the roles of intrinsic disorder in their functions.
Keywords: Sex determination, Sry pathway, intrinsically disordered proteins, protein-protein interactions, posttranslational modifications, binding induced folding, polymorphysm, protein structure, protein function.
Current Protein & Peptide Science
Title:Intrinsic Disorder in Male Sex Determination: Disorderedness of Proteins from the Sry Transcriptional Network
Volume: 18 Issue: 5
Author(s): Jean Merone, Onyekahi Nwogu, Jennifer M. Redington and Vladimir N. Uversky
Affiliation:
Keywords: Sex determination, Sry pathway, intrinsically disordered proteins, protein-protein interactions, posttranslational modifications, binding induced folding, polymorphysm, protein structure, protein function.
Abstract: Sex differentiation is a complex process where sexually indifferent embryo progressively acquires male or female characteristics via tightly controlled, perfectly timed, and sophisticatedly intertwined chain of events. This process is controlled and regulated by a set of specific proteins, with one of the first steps in sex differentiation being the activation of the Y-chromosomal Sry gene (sexdetermining region Y) in males that acts as a switch from undifferentiated gonad somatic cells to testis development. There are several key players in this process, which constitute the Sry transcriptional network, and collective action of which governs testis determination. Although it is accepted now that many proteins engaged in signal transduction as well as regulation and control of various biological processes are intrinsically disordered (i.e., do not have unique structure and remain unstructured, or incompletely structured, under physiological conditions), the roles and profusion of intrinsic disorder in proteins involved in the male sex determination have not been accessed as of yet. The goal of this study is to cover this gap by analyzing some key players of the Sry transcriptional network. To this end, we employed a broad set of computational tools for intrinsic disorder analysis and conducted intensive literature search in order to gain information on the structural peculiarities of the Sry networkrelated proteins, their intrinsic disorder predispositions, and the roles of intrinsic disorder in their functions.
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Cite this article as:
Merone Jean, Nwogu Onyekahi, Redington M. Jennifer and Uversky N. Vladimir, Intrinsic Disorder in Male Sex Determination: Disorderedness of Proteins from the Sry Transcriptional Network, Current Protein & Peptide Science 2017; 18 (5) . https://dx.doi.org/10.2174/1389203717666161028150244
DOI https://dx.doi.org/10.2174/1389203717666161028150244 |
Print ISSN 1389-2037 |
Publisher Name Bentham Science Publisher |
Online ISSN 1875-5550 |
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