Endosymbionts like Wolbachia influence the physiology and reproduction of their hosts, but successful transmission between generations is essential for their persistence, especially in Drosophila melanogaster.
Research reveals that cooling temperatures impact the abundance of the wMel variant of Wolbachia during key stages of fruit fly reproduction, explaining variations in its prevalence across different climates globally.
Genetic analyses show that temperature-sensitive traits, particularly a unique stop codon in a Wolbachia protein, adapt the wMel variant to thrive in temperate climates, suggesting potential for targeted use in biocontrol strategies against diseases transmitted by other insects.
The small β-barrel (SBB) is a versatile protein domain with a complex evolutionary background and a wide range of structural variations, playing key roles in numerous cellular processes.
The analysis examines the defining features of SBBs, including different naming systems and introduces the concept of an "urfold" to explain their structural diversity.
Many SBB proteins form cyclic oligomers that serve as functional units, demonstrating significant flexibility in their structure and function, leading to three main themes related to their versatile structure-function relationship.
Hfq is a vital bacterial protein that regulates gene expression after transcription by forming disc-like structures that bind different RNA molecules.
It helps facilitate interactions between small regulatory RNAs and their mRNA targets, making it an essential component in various regulatory networks linked to stress response and biofilm formation.
The chapter discusses methods for producing high-quality Hfq and RNA samples needed for crystallization and structural studies, highlighting the challenges in obtaining pure and homogeneous specimens.
The Hfq protein, part of the Sm family, plays a crucial role in regulating mRNA stability and expression by facilitating interactions between small regulatory RNAs (sRNAs) and their target mRNAs.
Hfq forms homo-hexameric rings with multiple RNA-binding surfaces, including a newly identified 'lateral rim' that aids in the pairing process, although its evolutionary significance is not fully understood.
Research on the Hfq from the thermophile Aquifex aeolicus revealed strong binding to specific RNA types and significant evolutionary conservation, setting the stage for more investigations into RNA interactions in ancient bacterial groups.