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Published on: July 29, 2019
Evolutionary and structural aspects of Solanaceae RNases T2
Claudia Elizabeth Thompson1, Lauís Brisolara-Corrêa2, Helen Nathalia Thompson3
1Universidade Federal de Ciências da Saúde de Porto Alegre, Departamento de Farmacociências, Porto Alegre, RS, Brazil.
Plant RNases T2, crucial for plant development and defense, show key amino acid variations. These differences in S-RNases and S-like RNases impact RNA binding and protein function.
Area of Science:
- Plant molecular biology
- Biochemistry
- Evolutionary biology
Background:
- Plant Ribonucleases T2 (RNases T2) are vital enzymes regulating diverse physiological and developmental processes.
- These processes include nutrient starvation, senescence, pathogen defense, and reproductive self-incompatibility.
- Solanaceae family RNases are classified into three main clades: S-RNases and two clades of S-like RNases.
Purpose of the Study:
- To investigate the evolutionary pressures and structural variations in plant RNases T2.
- To understand how amino acid differences in S-RNases and S-like RNases relate to their functions.
Main Methods:
- Comparative analysis of amino acid sequences to identify positively selected sites.
- Structural analysis focusing on flexible regions and substrate-binding sites.
Main Results:
- Identified several positively selected amino acids in flexible regions of S-RNases and S-like RNases.
- Highlighted differences in substrate-binding site flexibility between S-RNases and S-like RNases.
- Observed specific flexible sites in S-like RNase NT (Tyr156, Asn134) potentially involved in pathogen interactions.
Conclusions:
- Differential selective pressures drive amino acid variability in plant RNases T2.
- Structural variations, particularly in flexible substrate-binding regions, are crucial for the distinct functions of S-RNases and S-like RNases.
- These variations likely facilitate diverse RNA-binding interactions, including responses to viral infections.
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