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Results: 8

1.
Fig 4

Fig 4. From: Multiple Roles for Acetylation in the Interaction of p300 HAT with ATF-2.

Proposed model to explain enhanced affinity of p300 HAT for ATF-2-b-ZIP for hyperacetylated p300 HAT.

Balasubramanyam Karanam, et al. Biochemistry. ;46(28):8207-8216.
2.
Fig 1

Fig 1. From: Multiple Roles for Acetylation in the Interaction of p300 HAT with ATF-2.

ATF-2 and p300 architecture. A) Domain structure of ATF-2. B) Schematic representation of p300 domain structure with selected interacting proteins.

Balasubramanyam Karanam, et al. Biochemistry. ;46(28):8207-8216.
3.
Fig 7

Fig 7. From: Multiple Roles for Acetylation in the Interaction of p300 HAT with ATF-2.

ATF-2 acetylation in cell culture. 293 and Cos 7 cells were treated with TNFα, cycloheximide, PMA, or HDAC inhibitors as indicated and ATF-2 was immunoprecipitated and blotted with anti-ATF-2 and anti-acetyl-Lys as indicated.

Balasubramanyam Karanam, et al. Biochemistry. ;46(28):8207-8216.
4.
Fig 2

Fig 2. From: Multiple Roles for Acetylation in the Interaction of p300 HAT with ATF-2.

Affinity binding assays with immobilized GST-ATF-2-b-ZIP. A) Comparative pull-downs of wt hyperacetylated p300 HAT, wt hypoacetylated p300 HAT, and hypoacetylated p300 HAT-Δloop. SDS-PAGE are stained with Coomassie and intensity values derived from duplicate measurements. B) Control experiments with lanes 1 and 3 employing resin only and GST bound to resin and lane 2 containing GST-ATF-2-b-ZIP each treated with hyperacetylated p300 HAT protein as in A.

Balasubramanyam Karanam, et al. Biochemistry. ;46(28):8207-8216.
5.
Fig 6

Fig 6. From: Multiple Roles for Acetylation in the Interaction of p300 HAT with ATF-2.

MALDI MS/MS spectra of two acetylated peptides obtained from the tryptic digest of the GST-ATF-2 b-ZIP domain: A) KAcFLER and B) KAcVWVQSLEK; the peaks labeled as KAc represents the characteristic ions of acetylated lysine residue. The y-series ions labeled on the spectra refer to cleavages at the peptide amide bonds with positive charge retention on the C-terminal fragment, according to the nomenclature by Biemann (46). C) Sequence of ATF-2 b-ZIP indicating acetylation sites at K357 and K374.

Balasubramanyam Karanam, et al. Biochemistry. ;46(28):8207-8216.
6.
Fig 5

Fig 5. From: Multiple Roles for Acetylation in the Interaction of p300 HAT with ATF-2.

ATF-2-b-ZIP is acetylated by p300 HAT. A) hypoacetylated p300 HAT-mediated acetylation of GST-ATF-2-b-ZIP (2.5 μM) vs. time with 40 nM p300 HAT (relative acetylation values at 0.5 min, 38%; 1 min, 50%, 2 min, 68%, and 4 min, 100%). B) Acetylation of GST-ATF-2-b-ZIP (5 μM) vs. GST (5 μM) by hypoacetylated p300 HAT (0 or 40 nM). C) Concentration dependence of acetylation of GST ATF-2-b-ZIP by hypoacetylated p300 HAT. D) Comparison of hyperacetylated p300 HAT and hypoacetylated p300 HAT catalyzed acetylation of GST-ATF-2-b-ZIP. GST-ATF-2-b-ZIP (5 μM) incubated with hyper/hypoacetylated p300 HAT domain (40 nM) for 4 min.

Balasubramanyam Karanam, et al. Biochemistry. ;46(28):8207-8216.
7.
Fig 3

Fig 3. From: Multiple Roles for Acetylation in the Interaction of p300 HAT with ATF-2.

ATF-2-b-ZIP domain inhibits hyperacetylated p300 activity A) Time course of hyperacetylated (left) or hypoacetylated p300 HAT (right) (40 nM) used to acetylate peptide H4-15 peptide (100 μM) in the presence of GST-ATF-2-b-ZIP domain (0, 1, 5 μM; black, blue, red, respectively). B) Replot of 30 s time point with hyperacetylated p300 HAT data in A (left) and control using 5 μM GST in place of GST-ATF-2-b-ZIP (right). C) Replot of 30 s time point with hypoacetylated p300 HAT data in A (left) and control using 5 μM GST in place of GST-ATF-2-b-ZIP (right).

Balasubramanyam Karanam, et al. Biochemistry. ;46(28):8207-8216.
8.
Fig 8

Fig 8. From: Multiple Roles for Acetylation in the Interaction of p300 HAT with ATF-2.

Mutational Analysis of Lys-357 and Lys-374 in ATF-2 on transcriptional regulation using a CREB luciferase reporter plasmid. A) Cell lysates were analyzed for luciferase activity. The bars from left to right are as follows: C-control; CRE–pCRE-luc plasmid alone; Renilla- Renilla plasmid alone; Wt-ATF-2, pCRE-luc, Renilla together (as for all of the ATF-2 mutants to the right of Wt); KKRR-double lysine to arginine mutant; K357R; K357A; K357Q; K374Q; KKAA-double lysine to alanine mutant; KKQQ-double lysine to glutamine mutant; K374R; K374A. Anti-ATF-2 immunoblots show comparable transfection efficiency and ATF-2 stability in overexpressing conditions. B) Sequence alignment of acetylated lysines-357 and 374 in human ATF-2 b-ZIP domain show partial or full conservation in related transcription factors human CREB5, human ATF3, and chicken ATF-2.

Balasubramanyam Karanam, et al. Biochemistry. ;46(28):8207-8216.

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