Structural identification of putative USPs in Catharanthus roseus.

Area of Science:

• Molecular Biology
• Bioinformatics
• Plant Science

Background:

• Universal stress proteins (USPs) are crucial for cellular adaptation to environmental stress.
• Understanding USP diversity and function in plants like C. roseus is vital for crop resilience.
• Previous studies have characterized USPs in various organisms, but plant-specific architectures remain less explored.

Purpose of the Study:

• To identify and characterize putative universal stress proteins (USPs) in C. roseus.
• To analyze the domain architectures and evolutionary relationships of C. roseus USPs.
• To investigate the sequence conservation and potential ATP-binding capabilities of USPA-like domains.

Main Methods:

• Assembly and translation of nucleotide sequences from the C. roseus SRA database.
• Detection of Pfam putative USPA proteins and domain analysis (USPA, PK-like, (tyr)PK-like, U-box, TPR, apoLp-III, Cdc37).
• Multiple sequence alignment and phylogenetic tree construction to assess sequence conservation and relationships.

Main Results:

• Identified 24 putative USPA proteins in C. roseus, organized into six distinct architectures.
• Confirmed the presence of the USPA-like domain in all architectures, often associated with PK-like, (tyr)PK-like, U-box, TPR, apoLp-III, or Cdc37 domains.
• Phylogenetic analysis revealed high sequence conservation between plant (C. roseus) and bacterial USPA-like domains, with distinct grouping patterns.

Conclusions:

• C. roseus possesses a diverse repertoire of USP architectures, suggesting complex roles in stress response.
• The identified USPA-like domains exhibit conserved features with bacterial homologs, including potential ATP-binding sites.
• This study provides foundational insights into plant USP evolution and functional diversification.