High impact information on EGD2

• The yeast nascent polypeptide-associated complex (NAC) is encoded by two genes, EGD1 and EGD2, and is associated with cytoplasmic ribosomes [1].
• In vitro binding studies suggested that binding of j4R to alpha NAC did not interfere with the binding of alpha- and beta NAC subunits (the BTF3 transcription factor) [2].
• Confocal microscopy indicated that a proportion of j4R and alpha NAC interact in areas close to the plasma membrane, as well as through the cytoplasm in cells [2].
• Ribosome nascent chains (RNCs) of the two naturally occurring invertase species (secreted or cytosolic) were prepared in wild-type, delta alpha NAC or delta alpha beta 1 beta 3 NAC translation lysates and tested for binding to the corresponding microsomal membranes [3].
• The lack of phenotype, the high levels of EGD1 and EGD2 expression, and the identification of multiple human genes encoding NAC subunits suggest that the yeast EGD genes may be members of multigene families with redundant function [4].

Biological context of EGD2

• Disruption of EGD2, alone or in combination with an EGD1 disruption, causes no obvious phenotypes [4].
• In this work, we determine that the Saccharomyces cerevisiae Ccr4-Not complex controls ubiquitination of the conserved ribosome-associated heterodimeric EGD (enhancer of Gal4p DNA binding) complex, which consists of the Egd1p and Egd2p subunits in yeast and is named NAC (nascent polypeptide-associated complex) in mammals [5].

Associations of EGD2 with chemical compounds

• We have cloned and characterized EGD2 encoding the 27-kDa protein and found that Egd2p is strikingly similar to the alpha subunit of human NAC [4].

References