PMID- 21370068
OWN - NLM
STAT- MEDLINE
DCOM- 20110610
LR  - 20131121
IS  - 1940-6029 (Electronic)
IS  - 1064-3745 (Linking)
VI  - 723
DP  - 2011
TI  - A functional protein microarray approach to characterizing posttranslational 
      modifications on lysine residues.
PG  - 213-23
LID - 10.1007/978-1-61779-043-0_14 [doi]
AB  - Functional protein microarrays offer a versatile platform to address diverse 
      biological questions. Printing individually purified proteins in a spatially 
      addressable format makes it straightforward to investigating binary interactions. 
      To connect substrates to their upstream modifying enzymes, such as kinases, 
      ubiqutin (Ub) ligases, SUMOylation E3 ligases, and acetyltransferases, is an 
      especially daunting task using traditional methodologies. In recent years, 
      regulation via various types of posttranslational modifications (PTMs) on lysine 
      residues is emerging as an important mechanism(s) underlining diverse biological 
      -processes. Our group has been developing and applying functional protein 
      microarrays constructed for different model organisms to globally identify 
      enzyme-substrate interactions with a focus on lysine PTMs. In particular, we have 
      characterized the pleiotropic functions of a ubiquitin E3 ligase, Rsp5, via 
      identification of its downstream substrates using a yeast proteome chip. Also, we 
      have identified nonhistone substrates of the acetyltransferase NuA4 complex in 
      yeast, and revealed that reversible acetylation on a metabolic enzyme affects a 
      glucose metabolism and contributes to life span. In this chapter, we will provide 
      detailed protocols for the investigation of ubiquitylation and acetylation. These 
      protocols are generally applicable for different organisms.
FAU - Jeong, Jun Seop
AU  - Jeong JS
AD  - Department of Pharmacology and Molecular Sciences, High Throughput Biology 
      Center, Johns Hopkins School of Medicine, Baltimore, MD, USA.
FAU - Rho, Hee-Sool
AU  - Rho HS
FAU - Zhu, Heng
AU  - Zhu H
LA  - eng
PT  - Journal Article
PT  - Research Support, N.I.H., Extramural
PL  - United States
TA  - Methods Mol Biol
JT  - Methods in molecular biology (Clifton, N.J.)
JID - 9214969
RN  - K3Z4F929H6 (Lysine)
SB  - IM
MH  - Acetylation
MH  - Animals
MH  - Glass/chemistry
MH  - Lysine/metabolism
MH  - Printing
MH  - Protein Array Analysis/*methods
MH  - *Protein Processing, Post-Translational
MH  - Ubiquitination
EDAT- 2011/03/04 06:00
MHDA- 2011/06/11 06:00
CRDT- 2011/03/04 06:00
PHST- 2011/03/04 06:00 [entrez]
PHST- 2011/03/04 06:00 [pubmed]
PHST- 2011/06/11 06:00 [medline]
AID - 10.1007/978-1-61779-043-0_14 [doi]
PST - ppublish
SO  - Methods Mol Biol. 2011;723:213-23. doi: 10.1007/978-1-61779-043-0_14.