S. cerevisiae yeast Histone H2A blocking peptide (DAG-P2298)

Synthetic S. cerevisiae yeast Histone H2A blocking peptide for BL

Product Overview
S. cerevisiae yeast Histone H2A (unmodified ) peptide
Nature
Synthetic
Tag/Conjugate
Unconjugated
Cellular Localization
Nuclear
Procedure
None
Format
Liquid
Buffer
Information available upon request.
Preservative
None
Storage
Shipped at 4°C. Upon delivery aliquot and store at -20°C or -80°C. Avoid repeated freeze / thaw cycles. Information available upon request.
Introduction
Saccharomyces cerevisiae is a species of yeast. It is perhaps the most useful yeast, having been instrumental to winemaking, baking, and brewing since ancient times. It is believed that it was originally isolated from the skin of grapes (one can see the y
Antigen Description
Histones are basic nuclear proteins that are responsible for the nucleosome structure of the chromosomal fiber in eukaryotes. Nucleosomes consist of approximately 146 bp of DNA wrapped around a histone octamer composed of pairs of each of the four core histones (H2A, H2B, H3, and H4). The chromatin fiber is further compacted through the interaction of a linker histone, H1, with the DNA between the nucleosomes to form higher order chromatin structures. Linker histones are involved in the formation of higher order structure in chromatin and the maintenance of overall chromatin compaction. Whilst the core histones are highly conserved across a wide range of organisms, the linker histones are less conserved.
Keywords
H2A histone family member A; H2A.1; H2A.2; H2A/a; H2AFA; HIST1H2AE; Histone 1 H2ae; S. cerevisiae yeast Histone H2A; Saccharomyces cerevisiae yeast Histone H2A

Citations


Have you cited DAG-P2298 in a publication? Let us know and earn a reward for your research.

Customer Reviews


Write a review, share your experiences with others and get rewarded !
Product Name Cat. No. Applications Host Species Datasheet Price Add to Basket
Product Name Cat. No. Applications Host Species Datasheet Price Add to Basket

References


Hsl7p, the yeast homologue of human JBP1, is a protein methyltransferase

BIOCHEMICAL AND BIOPHYSICAL RESEARCH COMMUNICATIONS

Authors: Lee, JH; Cook, JR; Pollack, BP; Kinzy, TG; Norris, D; Pestka, S

The yeast protein Hsl7p is a homologue of Janus kinase binding protein 1, JBP1, a newly characterized protein methyltransferase. In this report, Hsl7p also is shown to be a methyltransferase. It can be crosslinked to [H-3]S-adenosylmethionine and exhibits in vitro protein methylation activity. Calf histones H2A and H4 and bovine myelin basic protein were methylated by Hsl7p, whereas histones H1, H2B, and H3 and bovine cytochrome c were not. We demonstrated that JBP1 can complement Saccharomyces cerevisiae with a disrupted HSL7 gene as judged by a reduction of the elongated bud phenotype, and a point mutation in the JBP1 S-adenosylmethionine consensus binding sequence eliminated all complementation by JBP1. Therefore, we conclude the yeast protein Hsl7p is a sequence and functional homologue of JBP1. These data provide evidence for an intricate link between protein methylation and macroscopic changes in yeast morphology. (C) 2000 Academic Press.

Regulation of chromosome stability by the histone H2A variant Htz1, the Swr1 chromatin remodeling complex, and the histone acetyltransferase NuA4

PROCEEDINGS OF THE NATIONAL ACADEMY OF SCIENCES OF THE UNITED STATES OF AMERICA

Authors: Krogan, NJ; Baetz, K; Keogh, MC; Datta, N; Sawa, C; Kwok, TCY; Thompson, NJ; Davey, MG; Pootoolal, J; Hughes, TR; Emili, A; Buratowski, S; Hieter, P; Greenblatt, JF

NuA4, the only essential histone acetyltransferase complex in Saccharomyces cerevisiae, acetylates the N-terminal tails of histones H4 and H2A. Affinity purification of NuA4 revealed the presence of three previously undescribed subunits, Vid2l/Eaf1/Ydr359c, Swc4/Eaf2/Ygr002c, and Eaf7/Ynl136w. Experimental analyses revealed at least two functionally distinct sets of polypeptides in NuA4: (i) Vid21 and Yng2, and (ii) Eaf5 and Eaf7. Vid21 and Yng2 are required for bulk histone H4 acetylation and are functionally linked to the histone H2A variant Htz1 and the Swr1 ATPase complex (SWR-C) that assembles Htz1 into chromatin, whereas Eaf5 and Eaf7 have a different, as yet undefined, role. Mutations in Htz1, the SWR-C, and NuA4 cause defects in chromosome segregation that are consistent with genetic interactions we have observed between the genes encoding these proteins and genes encoding kinetochore components. Because SWR-C-dependent recruitment of Htz1 occurs in both transcribed and centromeric regions, a NuA4/SWR-C/Htz1 pathway may regulate both transcription and centromere function in S. cerevisiae.

Online Inquiry

Name:
Phone: *
E-mail Address: *
Technology Interest:
Type of Organization:
Service & Products Interested: *
Project Description:

Related Products

Related Resources

Ordering Information

Payment methods we support:
Invoice / Purchase Order
Credit card

Inquiry Basket