Asset Details
Do you wish to reserve the book?
Structural basis of the Sir1-origin recognition complex interaction in transcriptional silencing
Hey, we have placed the reservation for you!
By the way, why not check out events that you can attend while you pick your title.
Oops! Something went wrong.
Looks like we were not able to place the reservation. Kindly try again later.
Are you sure you want to remove the book from the shelf?
Structural basis of the Sir1-origin recognition complex interaction in transcriptional silencing
Do you wish to request the book?
Structural basis of the Sir1-origin recognition complex interaction in transcriptional silencing
Please be aware that the book you have requested cannot be checked out. If you would like to checkout this book, you can reserve another copy
We have requested the book for you!
Your request is successful and it will be processed during the Library working hours. Please check the status of your request in My Requests.
Oops! Something went wrong.
Looks like we were not able to place your request. Kindly try again later.
Journal Article
Structural basis of the Sir1-origin recognition complex interaction in transcriptional silencing
2005
Overview
The Sir1 protein plays a key role in establishing a silent chromatin structure at the cryptic mating-type loci HMR and HML in Saccharomyces cerevisiae by interacting with the bromo-adjacent homology (BAH) domain of the Orc1p subunit of the origin recognition complex (ORC). Here, we present the high-resolution crystal structures of the ORC interaction region (OIR) of Sir1p and that of the complex formed between the OIR and BAH domains. Amino acids within the OIR previously shown to be required for a Sir1p/ORC interaction are presented on a conserved, convex surface that forms a complementary interface with a concave region of the Orc1 BAH domain that is critical for transcriptional silencing. The OIR/BAH interaction surface comprises a network of hydrophobic and polar/ionic interactions between discrete structural modules in each protein and involves several residues that were not implicated in previous studies. These data provide important structural insights into a protein-protein interaction critical for the formation of a specialized chromatin domain within eukaryotic chromosomes.
Publisher
National Academy of Sciences,National Acad Sciences
Subject
/ Conserved Sequence - genetics
/ Crystals
/ DNA-Binding Proteins - metabolism
/ Proteins
/ Saccharomyces cerevisiae - genetics
/ Saccharomyces cerevisiae - metabolism
/ Saccharomyces cerevisiae Proteins
/ Silent Information Regulator Proteins, Saccharomyces cerevisiae - chemistry
/ Silent Information Regulator Proteins, Saccharomyces cerevisiae - genetics
/ Silent Information Regulator Proteins, Saccharomyces cerevisiae - metabolism
/ Yeast
/ yeasts
