Department of Chemistry, University of Virginia, Charlottesville, VA 22904, USA.
Department of Biology, University of Victoria, Victoria, BC V8W 2Y2, Canada.
Biochem Cell Biol. 2024 Jun 1;102(3):238-251. doi: 10.1139/bcb-2023-0363. Epub 2024 Feb 26.
Insects are the largest group of animals when it comes to the number and diversity of species. Yet, with the exception of , no information is currently available on the primary structure of their sperm nuclear basic proteins (SNBPs). This paper represents the first attempt in this regard and provides information about six species of Neoptera: , and . The SNBPs of these species were characterized by acetic acid urea gel electrophoresis (AU-PAGE) and high-performance liquid chromatography fractionated. Protein sequencing was obtained using a combination of mass spectrometry sequencing, Edman N-terminal degradation sequencing and genome mining. While the SNBPs of several of these species exhibit a canonical arginine-rich protamine nature, a few of them exhibit a protamine-like composition. They appear to be the products of extensive cleavage processing from a precursor protein which are sometimes further processed by other post-translational modifications that are likely involved in the chromatin transitions observed during spermiogenesis in these organisms.
昆虫在物种的数量和多样性方面是最大的动物群体。然而，除了鳞翅目之外，目前还没有关于它们精子核碱性蛋白（SNBPs）的一级结构的信息。本文代表了在这方面的首次尝试，并提供了关于六种新翅目昆虫的信息：直翅目、蜚蠊目、革翅目、等翅目、半翅目和鞘翅目。这些物种的 SNBPs 通过乙酸尿素凝胶电泳（AU-PAGE）和高效液相色谱分级进行了表征。通过质谱测序、Edman N 末端降解测序和基因组挖掘的组合获得了蛋白质测序。虽然这些物种中的一些 SNBPs 表现出典型的富含精氨酸的鱼精蛋白性质，但其中一些表现出类似于鱼精蛋白的组成。它们似乎是前体蛋白经过广泛切割处理的产物，这些蛋白有时会进一步经过其他翻译后修饰，这些修饰可能参与了这些生物精子发生过程中观察到的染色质转变。
