Bioinformatics and experimental approaches identify families of membrane proteins requiring the co-ordinated action of the Sec pathway and Tat pathways for their integration and define features of the polypeptides that mediate interaction with these pathways.
In Escherichia coli structural maintenance of chromosomes (SMC) complex, MukBEF, a dimeric MukF kleisin binds and activates MukB SMC ATPases through two independent interfaces provided by distinct MukF N- and C-terminal domains.
Structure-function analysis of the super elongation complex formed when HIV replicates inside cells reveals that the HIV-1 Tat protein binds to a cleft between P-TEFb, an enzyme that is involved in normal transcription, and AFF4, a protein that is used to build the super elongation complex
Developmental genetic and cell culture studies indicate that the Inhibitor of DNA-binding protein Extra macrochaetae (Emc), previously thought to determine where bHLH proteins can act, is itself regulated by those bHLH dimerization partners at the level of protein stability.
In invertebrate and vertebrate models of Spinal Muscular Atrophy, diminished SMN protein causes Gemin3-dependent decreases in microRNA function, leading to upregulated M2 muscarinic receptor and deleterious consequences.