The Rpd3L histone deacetylase (HDAC) complex is an ancient 12-subunit complex conserved in a broad range of eukaryotes that performs localized deacetylation at or near sites of recruitment by DNA-bound factors. Here we describe the cryo-EM structure of this prototypical HDAC complex that is characterized by as many as seven subunits performing scaffolding roles for the tight integration of the only catalytic subunit, Rpd3. The principal scaffolding protein, Sin3, along with Rpd3 and the histone chaperone, Ume1, are present in two copies, with each copy organized into separate lobes of an asymmetric dimeric molecular assembly.
View Article and Find Full Text PDFNosocomial isolates of Pseudomonas aeruginosa exhibit high rates of resistance to antibiotics, and are often multidrug resistant. P. aeruginosa clinical isolates (n = 56) were obtained from ICU patients in a hospital in Pakistan over a 3-y period.
View Article and Find Full Text PDFJ Coll Physicians Surg Pak
March 2004
Objective: To determine the presence of Helicobacter pylori (H. pylori) infection, in patients suffering from gastritis and peptic ulcer disease by polymerase chain reaction (PCR) and correlate the results with the histological diagnosis.
Design: Analytical, comparative study.