<p>Charged Clusters (CC), subclasses of Intrinsically Disordered Protein Regions (IDPR), are vital for protein function by mediating electrostatic interactions, metal binding, and serving as hotspots for post-translational modifications. The evolutionary and functional constraints driving the Conserved CC (CCC) and their role as potentially important regions within IDPR are poorly understood. This study aimed to identify and analyze Positive and Negative CCC (PCCC and NCCC) across green plant species. Conservation rates for non-redundant CCC ranged between 9.8% and 20.9% intra and interspecies. Protein disorder is highly conserved in green plants, with disorder ratios and binding-induced order varying between intra and interspecies. The CCC sequence disorder ranged from 0 to 1 across categories, highlighting variable order-disorder dynamics. Sequence conservation patterns were kingdom- and proteome-specific, showing higher CCC in nuclear-encoded proteins versus mitochondrial-encoded ones and greater recurrence in land plants compared to green algae, reflecting eukaryotic regulatory complexity. Intraspecies NCCC were characterized by high tyrosine content, while PCCC were enriched in proline, balancing structural stability and functional specificity. CCC motifs correlated with key functional sites, including phosphorylation and metal-binding regions. Sequence-based clustering grouped proteins by molecular function rather than taxonomy, suggesting conservation of functional motifs across lineages and possible duplication-related diversification. This clustering reflects adaptive diversification linked to critical biological roles, especially in mitochondria. Overall, this study represents CCC as conserved regions within IDPR, potentially indicative of important functional roles, implicating them in cellular regulation, and offering a novel framework for protein classification and potential targets for protein engineering.</p>

错误:搜索内容不能为空,请输入英文关键词
错误:关键词超出字数限制,请精简
高级检索

Sequence Conservation and Functional Significance of Charged Clusters in Mitochondria-Located Proteins of Green Plants

  • Syrine Nebli,
  • Ahmed Rebai,
  • Imen Ayadi

摘要

Charged Clusters (CC), subclasses of Intrinsically Disordered Protein Regions (IDPR), are vital for protein function by mediating electrostatic interactions, metal binding, and serving as hotspots for post-translational modifications. The evolutionary and functional constraints driving the Conserved CC (CCC) and their role as potentially important regions within IDPR are poorly understood. This study aimed to identify and analyze Positive and Negative CCC (PCCC and NCCC) across green plant species. Conservation rates for non-redundant CCC ranged between 9.8% and 20.9% intra and interspecies. Protein disorder is highly conserved in green plants, with disorder ratios and binding-induced order varying between intra and interspecies. The CCC sequence disorder ranged from 0 to 1 across categories, highlighting variable order-disorder dynamics. Sequence conservation patterns were kingdom- and proteome-specific, showing higher CCC in nuclear-encoded proteins versus mitochondrial-encoded ones and greater recurrence in land plants compared to green algae, reflecting eukaryotic regulatory complexity. Intraspecies NCCC were characterized by high tyrosine content, while PCCC were enriched in proline, balancing structural stability and functional specificity. CCC motifs correlated with key functional sites, including phosphorylation and metal-binding regions. Sequence-based clustering grouped proteins by molecular function rather than taxonomy, suggesting conservation of functional motifs across lineages and possible duplication-related diversification. This clustering reflects adaptive diversification linked to critical biological roles, especially in mitochondria. Overall, this study represents CCC as conserved regions within IDPR, potentially indicative of important functional roles, implicating them in cellular regulation, and offering a novel framework for protein classification and potential targets for protein engineering.