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Protein & Peptide Letters

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ISSN (Print): 0929-8665
ISSN (Online): 1875-5305

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Research Article

Carboxyl Terminus of HOATZ is Intrinsically Disordered and Interacts with Heat Shock Protein A Families

Author(s): Keishi Narita* and Takuji Oyama

Volume 29, Issue 11, 2022

Published on: 12 October, 2022

Page: [971 - 978] Pages: 8

DOI: 10.2174/0929866529666220912115544

Price: $65

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Abstract

Background: Hoatz is a vertebrate-specific gene, the defects of which result in hydrocephalus and oligo-astheno-teratozoospermia in mice. It encodes a 19-kDa protein lacking any domains of known function.

Methods: To understand the protein activity, we purified the carboxyl-terminal fragment that is conserved among different species, and analyzed its structure and potential binding proteins. A soluble 9.9-kDa HOATZ fragment, including a poly-histidine tag (designated HOATZ-C), was purified to homogeneity.

Results: The gel filtration profile and circular dichroism spectra collectively indicated that HOATZ-C was intrinsically disordered. When HOATZ-C was mixed with cleared lysate from Hoatz-null mouse testis, several proteins, including two of ~70 kDa size, were specifically co-purified with HOATZ-C on a nickel column.

Conclusion: Based on the peptide mass fingerprinting of these bands, two members of the heat-shock protein family A were identified. These data may indicate the role of HOATZ in stress regulation in cells characterized by motile cilia and flagella.

Keywords: Motile cilia, flagella, circular dichroism, stress regulation, heat shock protein

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