The digestion of basic proteins by extract of guerin tumor lysosomes

Farbiszewski, R; Rzeczycki, W

doi:10.1016/s0006-291x(75)80090-8

Cited by 5 publications

(1 citation statement)

References 5 publications

Supporting

Mentioning

Contrasting

Order By: Relevance

“…Histone H1 was not detected in any of the pull‐down experiments. To confirm that the observed in vitro interaction was specific to histones, the experiments were repeated using GST‐4× MBT with either myelin basic protein (MBP) or bovine serum albumin (BSA) – two highly positively charged proteins that mimic histones [31,32]. In both cases, GST‐4× MBT failed to pull‐down MBP or BSA (Fig.…”

Section: Resultsmentioning

confidence: 96%

Human SFMBT is a transcriptional repressor protein that selectively binds the N‐terminal tail of histone H3

Trievel

Rice

2007

FEBS Letters

View full text Add to dashboard Cite

Human SFMBT (hSFMBT) is postulated to be a Polycomb (PcG) protein. Similar to other PcG proteins, we found that hSFMBT displays robust transcriptional repressor activity. In addition, hSFMBT localized to the nucleus where it strongly associates with chromatin by directly and selectively binding the N-terminal tail of histone H3. Importantly, we discovered that the four tandem MBT repeats of hSFMBT were sufficient for nuclear matrix-association, N-terminal tail H3 binding, and required for transcriptional repression. These findings indicate that the tandem MBT repeats form a functional structure required for biological activity of hSFMBT and predict similar properties for other MBT domain-containing proteins.

show abstract

Section: Resultsmentioning

confidence: 96%

Human SFMBT is a transcriptional repressor protein that selectively binds the N‐terminal tail of histone H3

Trievel

Rice

2007

FEBS Letters

View full text Add to dashboard Cite

show abstract

Characterization of cytoplasmic arginine-rich basic protein of Guerin epithelioma

Farbiszewski

Rzeczycki

1977

Mol Cell Biochem

View full text Add to dashboard Cite

Arginine-rich basic protein from cytoplasma of Guerin epitheliomas has been isolated and characterized. It contains five amino acids: arginine, lysine, glycine, alanine and glutamic acid which make together 74% of all amino acid residues. The protein has a cationic character with an isoelectric point of 8.2. No carbohydrate component was found in this protein. The significance of arginine-rich basic protein in the cytoplasma of Guerin epithelioma is discussed briefly.

show abstract