Sulfurtransferase and thioredoxin specifically interact as demonstrated by bimolecular fluorescence complementation analysis and biochemical tests
نویسندگان
چکیده
منابع مشابه
Sulfurtransferase and thioredoxin specifically interact as demonstrated by bimolecular fluorescence complementation analysis and biochemical tests
Sulfurtransferases (Strs) and thioredoxins (Trxs) are members of large protein families. Trxs are disulfide reductases and play an important role in redox-related cellular processes. They interact with a broad range of proteins. Strs catalyze the transfer of a sulfur atom from a suitable sulfur donor to nucleophilic sulfur acceptors in vitro, but the physiological roles of these enzymes are not...
متن کاملBimolecular fluorescence complementation.
Defining the subcellular distribution of signaling complexes is imperative to understanding the output from that complex. Conventional methods such as immunoprecipitation do not provide information on the spatial localization of complexes. In contrast, BiFC monitors the interaction and subcellular compartmentalization of protein complexes. In this method, a fluororescent protein is split into a...
متن کاملUpdate on Bimolecular Fluorescence Complementation in Plants The Analysis of Protein-Protein Interactions in Plants by Bimolecular Fluorescence Complementation
Following the complete genome sequencing of different plant species such as Arabidopsis (Arabidopsis thaliana), rice (Oryza sativa), and Physcomitrella (Physcomitrella patens), as well as advances toward deciphering entire proteomes, the need for a reliable way to identify protein-protein interactions is becoming a major task for the future. Bimolecular fluorescent complementation (BiFC) is a n...
متن کاملBimolecular fluorescence complementation analysis of eukaryotic fusion products
BACKGROUND INFORMATION Cell fusion is known to underlie key developmental processes in humans and is postulated to contribute to tissue maintenance and even carcinogenesis. The mechanistic details of cell fusion, especially between different cell types, have been difficult to characterize because of the dynamic nature of the process and inadequate means to track fusion products over time. Here ...
متن کاملDimerization of ABCG2 Analysed by Bimolecular Fluorescence Complementation
ABCG2 is one of three human ATP binding cassette transporters that are functionally capable of exporting a diverse range of substrates from cells. The physiological consequence of ABCG2 multidrug transport activity in leukaemia, and some solid tumours is the acquisition of cancer multidrug resistance. ABCG2 has a primary structure that infers that a minimal functional transporting unit would be...
متن کاملذخیره در منابع من
با ذخیره ی این منبع در منابع من، دسترسی به آن را برای استفاده های بعدی آسان تر کنید
ژورنال
عنوان ژورنال: FEBS Open Bio
سال: 2015
ISSN: 2211-5463
DOI: 10.1016/j.fob.2015.10.001