A growing team of groundbreaking scientists around the world are now sharing their lab notebooks online
Background PRMT1 is the type I protein arginine methyltransferase (Fig.1) which mono- and asymmetrically dimethylates histone and nonhistone proteins, mainly in glycine and arginine-rich motifs and is involved in various cellular processes such as transcription, RNA processing, DNA repair, cell cycle or signal transduction (PMID:26612103). It is responsible for depositing over 90% of the total Read More …
Hi, I would like to share with you the details for cellular assay detecting interaction between histone deacetylase HDAC6 and ubiquitin, which is a unique property within the histone deacetylase family. HDAC6 is a member of the histone deacetylase family which deacetylate lysine residues of histone and non-histone proteins. It plays an important role in Read More …
Hi, Recently, I have started working on NanoBret PPI technology for chromatin factors and E3 ligases are here is one of the assays I developed. Background (source: PMID28179136). The repressive Nucleosome Remodeling and histone Deacetylation (NuRD) complex alters chromatin structure by coupling ATP-dependent remodeling activity with histone deacetylation function. It is composed of six different Read More …
Hi Here are the details of the assay I developed to measure interaction between USP5 and ubiquitin in cells. Ubiquitin specific peptidase 5 (USP5) belongs to the largest ubiquitin-specific protease (USP) subfamily and has a zinc finger at its N-terminal portion and two ubiquitin-associated domains in the large catalytic region that mediate polyubiquitin binding (PMID:28923280, Read More …
We have used the PTMScan® Mono-Methyl Arginine Motif [mme-RG] Kit #12235 from CST in order to determine novel PRMT7 substrates. In preliminary experiments done few years ago by our pharma partner several novel potential PRMT7 substrates were discovered with the kit, including HSP70, which was further validated by different methods (https://www.biorxiv.org/content/10.1101/503136v2). In order to obtain biological replicates, Read More …
My previous results showed that overexpression of HDAC11 decrease basal acetylation levels of exogenous histones as well as decrease the acetylation increase caused by histone acetyltransferases. In order to determine if the observed effect is caused by catalytic activity of HDAC11, I used catalytic HDAC11 mutants Y304H and H142,143A (PIMID: 30819897, 28927261) and published HDAC11 Read More …
In my previous post I mentioned that there is controversy if HDAC11 can deacetylate histones. I decided to look at the effect of overexpression of HDAC11 on exogenous histone acetylation in cells. In my preliminary results I noticed that exogenous GFP-tagged histones, one day post transfection, have very low levels of acetylation; therefore I decided Read More …
Hi Everyone, This is the first time I am going to share with you my research and I will start with the project I am currently working on, which is the development of cellular HDAC11 target engagement assay. HDAC11, the only member of class IV HDAC subfamily, was believed to be responsible for the deacetylation Read More …
