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1.
F <span style="font-variant: small-caps" class="small-caps">igure</span>  7.—

F igure 7.—. From: Histone H3 K56 Hyperacetylation Perturbs Replisomes and Causes DNA Damage.

hst3 hst4 cells require a Mec1p-dependent function for viability. (A) Synthetic lethality between hst3 hst4 and pol2-11. Serial dilutions (1:5) of strains ICY356 (WT), ICY674 (pol2-11), ICY676 (pol2-11 hst3), ICY680 (pol2-11 hst4), ICY610 (hst3 hst4), and ICY682 (pol2-11 hst3 hst4) were spotted on SC −Ura and SC +FOA and grown for 3–4 days at 25°. (B) Synthetic lethality between hst3 hst4 and mec1 and dun1. Serial dilutions (1:5) of strains ICY356 (WT), ICY703 (hst3 hst4), ICY430 (hst3 hst4 sml1), ICY431 (hst3 hst4 sml1 mec1), ICY351 (hst3 hst4 sml1 rad53), and ICY230 (hst3 hst4 dun1) were spotted on SC −Ura and SC +FOA and grown for 3–4 days at 30°.

Ivana Celic, et al. Genetics. 2008 August;179(4):1769-1784.
2.
F <span style="font-variant: small-caps" class="small-caps">igure</span>  5.—

F igure 5.—. From: Histone H3 K56 Hyperacetylation Perturbs Replisomes and Causes DNA Damage.

Like wild-type cells, hst3 hst4 cells slow down DNA replication and spindle elongation when exposed to MMS and HU, respectively. (A) ICY48 (bar1) and ICY49 (bar1 hst3 hst4) cells were arrested with α-factor and released into medium with and without MMS. Aliquots of the cells were taken at indicated time points and analyzed by FACS. (B–C) ICY48 (bar1) and ICY49 (bar1 hst3 hst4) cells were arrested with α-factor and released into medium with and without 100 mm HU. Aliquots of the cells were taken at indicated time points and analyzed by FACS (B) and immunofluorescence for tubulin staining (C).

Ivana Celic, et al. Genetics. 2008 August;179(4):1769-1784.
3.
F <span style="font-variant: small-caps" class="small-caps">igure</span>  8.—

F igure 8.—. From: Histone H3 K56 Hyperacetylation Perturbs Replisomes and Causes DNA Damage.

Synthetic lethality analysis with hst3 hst4 and suppression with H3 K56R. (A) Serial dilutions (1:5) of strains ICY356a (WT + vector), ICY703a (hst3 hst4 + vector), ICY703b (hst3 hst4 + HHT1), and ICY703c (hst3 hst4 + hht1K56R) were spotted on SC −Leu −Ura and SC −Leu +5-FOA and grown at the indicated temperatures for 2 and 3 days, respectively. (B) Serial dilutions (1:5) of strains ICY356a (WT + vector), ICY703a (hst3 hst4 + vector), ICY431a, -b, and -c, ICY1566a, -b, and -c, ICY1568a, -b, and -c, ICY1570a, -b, and -c, ICY1572a, -b, and -c, ICY682a, -b, and -c, ICY1574a, -b, and -c, and ICY1576a, -b, and -c were spotted on SC −Leu −Ura and SC −Leu +5-FOA and grown at the indicated temperatures for 2 and 3 days, respectively.

Ivana Celic, et al. Genetics. 2008 August;179(4):1769-1784.
4.
F <span style="font-variant: small-caps" class="small-caps">igure</span>  1.—

F igure 1.—. From: Histone H3 K56 Hyperacetylation Perturbs Replisomes and Causes DNA Damage.

Overexpression of RFC1 suppresses the growth defect, Ts phenotype, and sensitivity to genotoxic agents of hst3 hst4 cells. (A) Serial dilutions (1:5) of strains ICY188 (WT + YEP351), ICY189 (WT + YEP351/RFC1), ICY190 (hst3 hst4 + YEP351), and ICY191 (hst3 hst4 + YEP351/RFC1) were spotted on SC −Leu −Ura and SC −Leu +5-FOA and grown at the indicated temperatures for 2–3 days. (B) After shuffling out a URA3-marked plasmid on 5-FOA and an additional round of 5-FOA selection, the strains ICY188, ICY190, and ICY191 were spotted in serial dilutions (1:5) on SC −Leu and grown at 30° as indicated.

Ivana Celic, et al. Genetics. 2008 August;179(4):1769-1784.
5.
F <span style="font-variant: small-caps" class="small-caps">igure</span>  3.—

F igure 3.—. From: Histone H3 K56 Hyperacetylation Perturbs Replisomes and Causes DNA Damage.

Genetic interaction with ctf4 and ctf18. (A) Suppression of the hst3 hst4 Ts phenotype and HU sensitivity by deletion of CTF4. Serial dilutions (1:5) of strains ICY1488 (WT), ICY1676 (ctf4), ICY1514 (hst3 hst4), and ICY1684 (hst3 hst4 ctf4) were spotted on YPD and YPD + 100 mm HU and grown for 3 days at 25° and 37° (YPD) and 5 days at 25° (YPD + HU). (B) Analysis of genetic interaction between ctf4, ctf18, and hht1(K56R). Serial dilutions (1:5) of strains ICY1492 (hht2-hhf2), ICY1688 (hht2-hhf2 ctf4), ICY1605 (hht2-hhf2 ctf18), ICY1497 [hht2-hhf2 hht1(K56R)], ICY1692 [hht2-hhf2 hht1(K56R) ctf4], and ICY1607 [hht2-hhf2 hht1(K56R) ctf18] were spotted on YPD, YPD + 50 mm HU, and YPD + 1 μg/ml CPT and grown for 3 days (YPD) and 5 days (YPD + HU; YPD + CPT) at 25°.

Ivana Celic, et al. Genetics. 2008 August;179(4):1769-1784.
6.
F <span style="font-variant: small-caps" class="small-caps">igure</span>  2.—

F igure 2.—. From: Histone H3 K56 Hyperacetylation Perturbs Replisomes and Causes DNA Damage.

Suppression of the hst3 hst4 growth defect and Ts phenotype by inactivation of alternative RFC complexes. (A) Serial dilutions (1:5) of strains ICY356 (WT), ICY703 (hst3 hst4), ICY1528 (hst3 hst4 rad24), ICY1534 (hst3 hst4 elg1), ICY1537 (hst3 hst4 ctf18), ICY1544 (hst3 hst4 mec3), ICY1550 (hst3 hst4 rad17), ICY1556 (hst3 hst4 ddc1), ICY1797 (hst3 hst4 ctf8), ICY1795 (hst3 hst4 dcc1) were spotted on SC −Ura or SC +5-FOA and grown for 3 days at the indicated temperatures. (B) Serial dilutions (1:5) of strains ICY356 (WT), ICY252 (hst3 hst4), ICY342 (hst3 hst4 rad24), ICY449 (hst3 hst4 rad9), and ICY773 (hst3 hst4 rad9 rad24) were spotted on SC −Ura (25°), SC +5-FOA (25°), and SC +5-FOA (37°) and grown for 3 days at the indicated temperatures.

Ivana Celic, et al. Genetics. 2008 August;179(4):1769-1784.
7.
F <span style="font-variant: small-caps" class="small-caps">igure</span>  4.—

F igure 4.—. From: Histone H3 K56 Hyperacetylation Perturbs Replisomes and Causes DNA Damage.

Analysis of K56 acetylation. (A) Total protein extracts were prepared from strains ICY188 (WT + YEP351), ICY190 (hst3 hst4 + YEP351), ICY191 (hst3 hst4 + YEP351/RFC1), and ICY192 (hst3 hst4 + YEP351/RFC1) after two rounds of 5-FOA selection to lose the URA3 (WT) and URA3-HST3 (hst3 hst4 strains) plasmids, and the acetylation of histone H3 K56 was analyzed by immunoblotting with a K56Ac-specific antibody. The membrane was stripped and reprobed with an antibody specific for the C terminus of H3. (B) Total protein extracts from strains ICY1488 (WT), ICY1514 (hst3 hst4), ICY1646 (hst3 hst4 rad24), ICY1664 (hst3 hst4 elg1), ICY1613 (hst3 hst4 ctf18), ICY1684 (hst3 hst4 ctf4), and ICY1216 (asf1) were separated by SDS–PAGE and immunoblotted with a K56Ac specific antibody. The membrane was stripped and reprobed with an antibody specific for the C terminus of H3.

Ivana Celic, et al. Genetics. 2008 August;179(4):1769-1784.
8.
F <span style="font-variant: small-caps" class="small-caps">igure</span>  6.—

F igure 6.—. From: Histone H3 K56 Hyperacetylation Perturbs Replisomes and Causes DNA Damage.

Induction of RNR3 and HUG1 and hyperphosphorylation of Rad53p in hst3 hst4 cells. (A) Total RNA was isolated from strains YCB617 (WT), YCB470 (hst3), YCB575 (hst4), ICY252 (hst3 hst4), ICY342 (hst3 hst4 rad24), ICY449 (hst3 hst4 rad9), and ICY773 (hst3 hst4 rad9 rad24) and hybridized to RNR3, HUG1, and actin-specific probes. Prior to the experiment, strains ICY252, 342, 449, and 773 were grown on 5-FOA to shuffle out a URA3 plasmid carrying the HST3 gene. (B) Rad53p is hyperphosphorylated in a Rad24p- and Rad9p-dependent manner in hst3 hst4 cells, but not in the single mutants. Total protein extracts from the strains YCB617 (WT), YCB470 (hst3), YCB575 (hst4), ICY252 (hst3 hst4), ICY342 (hst3 hst4 rad24), ICY449 (hst3 hst4 rad9), and ICY773 (hst3 hst4 rad9 rad24) were separated by SDS–PAGE and immunoblotted with an antibody specific for Rad53p. Prior to the experiment, strains ICY252, 342, 449, and 773 were grown on 5-FOA to shuffle out a URA3 plasmid carrying the HST3 gene. (C) H3 K56R mutation reduces Rad53p phosphorylation in hst3 hst4 strains. Total protein extracts were prepared from strains ICY1488 (WT), ICY1514 (hst3 hst4), ICY1518 (hst3 hst4 hht1K56R), ICY1492 (hht2-hhf2), ICY1497 (hht2-hhf2 hht1K56R), ICY1501 (hht2-hhf2 hst3 hst4), and ICY1506 (hht2-hhf2 hht1K56R hst3 hst4) and analyzed for Rad53p phosphorylation using a Rad53p-specific antibody.

Ivana Celic, et al. Genetics. 2008 August;179(4):1769-1784.

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