Molecular Basis for Chaperone Control of Rtt109 Acetylation of Histone H3-H4

N Akhavantabib - 2021 - utd-ir.tdl.org
Acetylation is one of many protein post-translational modifications (PTMs) that frequently
occurs in the cell. One type of acetylation is when the acetyl group from acetyl-coenzyme A …

The carboxyl terminus of Rtt109 functions in chaperone control of histone acetylation

E Radovani, M Cadorin, T Shams, S El-Rass… - Eukaryotic …, 2013 - Am Soc Microbiol
Rtt109 is a fungal histone acetyltransferase (HAT) that catalyzes histone H3 acetylation
functionally associated with chromatin assembly. Rtt109-mediated H3 acetylation involves …

[HTML][HTML] Structure and histone binding properties of the Vps75-Rtt109 chaperone-lysine acetyltransferase complex

D Su, Q Hu, H Zhou, JR Thompson, RM Xu… - Journal of Biological …, 2011 - ASBMB
The histone chaperone Vps75 presents the remarkable property of stimulating the Rtt109-
dependent acetylation of several histone H3 lysine residues within (H3-H4) 2 tetramers. To …

[HTML][HTML] Utilizing targeted mass spectrometry to demonstrate Asf1-dependent increases in residue specificity for Rtt109-Vps75 mediated histone acetylation

YM Kuo, RA Henry, L Huang, X Chen, LA Stargell… - PloS one, 2015 - journals.plos.org
In Saccharomyces cerevisiae, Rtt109, a lysine acetyltransferase (KAT), associates with a
histone chaperone, either Vps75 or Asf1. It has been proposed that these chaperones alter …

[PDF][PDF] Structure of the Rtt109-AcCoA/Vps75 complex and implications for chaperone-mediated histone acetylation

Y Tang, MA Holbert, N Delgoshaie, H Wurtele… - Structure, 2011 - cell.com
Yeast Rtt109 promotes nucleosome assembly and genome stability by acetylating K9, K27,
and K56 of histone H3 through interaction with either of two distinct histone chaperones …

Molecular functions of the histone acetyltransferase chaperone complex Rtt109–Vps75

CE Berndsen, T Tsubota, SE Lindner, S Lee… - Nature structural & …, 2008 - nature.com
Histone acetylation and nucleosome remodeling regulate DNA damage repair, replication
and transcription. Rtt109, a recently discovered histone acetyltransferase (HAT) from …

Understanding histone acetyltransferase Rtt109 structure and function: how many chaperones does it take?

S D'Arcy, K Luger - Current opinion in structural biology, 2011 - Elsevier
Rtt109 (Regulator of Ty1 Transposition 109) is a fungal-specific histone acetyltransferase
required for modification of histone H3 K9, K27 and K56. These acetylations are associated …

Catalytic activation of histone acetyltransferase Rtt109 by a histone chaperone

EM Kolonko, BN Albaugh, SE Lindner… - Proceedings of the …, 2010 - National Acad Sciences
Most histone acetyltransferases (HATs) function as multisubunit complexes in which
accessory proteins regulate substrate specificity and catalytic efficiency. Rtt109 is a …

Kinetic mechanism of the Rtt109− Vps75 histone acetyltransferase− chaperone complex

BN Albaugh, EM Kolonko, JM Denu - Biochemistry, 2010 - ACS Publications
Rtt109 is a histone acetyltransferase (HAT) involved in promoting genomic stability, DNA
repair, and transcriptional regulation. Rtt109 associates with the NAP1 family histone …

Interaction with the Histone Chaperone Vps75 Promotes Nuclear Localization and HAT Activity of Rtt109 In Vivo

KM Keck, LF Pemberton - Traffic, 2011 - Wiley Online Library
Modification of histones is critical for the regulation of all chromatin‐templated processes.
Yeast Rtt109 is a histone acetyltransferase (HAT) that acetylates H3 lysines 9, 27 and 56 …