Plant cells contain a mixture of 26S and 20S proteasomes that mediate ubiquitin dependent
and ubiquitin independent proteolysis, respectively. The 26S proteasome contains the 20S …

Proteasomes are large multisubunit, multicatalytic proteases responsible for most of the
cytosolic and nuclear protein degradation, and their structure and functions are conserved in …

Selective proteolysis in plants is largely mediated by the ubiquitin (Ub)/proteasome system
in which substrates, marked by the covalent attachment of Ub, are degraded by the 26 S …

Plants use a repertoire of methods to control the level and activity of their constituent
proteins. One method, whose prominence is only now being appreciated, is selective protein …

Summary The 26S proteasome (26SP) is a multi‐subunit, multi‐catalytic protease that is
responsible for most of the cytosolic and nuclear protein turnover. The 26SP is composed of …

Proteotoxic stress, which is generated by the accumulation of unfolded or aberrant proteins
due to environmental or cellular perturbations, can be mitigated by several mechanisms …

The ubiquitin 26S proteasome (26SP) system efficiently degrades many key regulators of
plant development. 26SP consists of two subcomplexes: the catalytic 20S core particle (CP) …

Ubiquitin is a small, highly conserved, ubiquitously expressed eukaryotic protein with
immensely important and diverse regulatory functions. A well-studied function of ubiquitin is …

A tightly regulated and highly specific system for the degradation of individual proteins is
essential for the survival of all organisms. In eukaryotes, this is achieved by the tagging of …

The 26S proteasome is an essential protease complex responsible for removing most short-
lived intracellular proteins, especially those modified with polyubiquitin chains. We show …