17:
89:
The three subunits work together to make the complex function. The human subunit (p150) interacts with PCNA, which acts as a sliding clamp, to help the CAF-1 complex interact with the DNA replication fork. Additionally, p150 along with PCNA performs nucleotide excision repair to fix any damaged DNA.
97:
A mutation in p150 that results in a loss of function would lead to double stranded breaks, interruptions in the replication fork and translocations. In p60, loss of function would mean the histone chaperone for H3/H4 would not interact with the complex. A mutation like this in either subunit would
93:
p60 attracts ASF1a/b which is a chaperone for H3/H4 and this is in the complex with p150 which interacts with PCNA to attach to the replication fork. The CAF-1 complex adds the histones to the DNA ahead of the replication fork.
629:
Ishiuchi T, Enriquez-Gasca R, Mizutani E, Bošković A, Ziegler-Birling C, Rodriguez-Terrones D, et al. (September 2015). "Early embryonic-like cells are induced by downregulating replication-dependent chromatin assembly".
98:
result in loss of function for the CAF-1 complex as a whole. However, loss of function in p48 would alter how well the complex is able to chaperone chromatin, but would not stop it as a whole.
206:
Smith S, Stillman B (July 1989). "Purification and characterization of CAF-I, a human cell factor required for chromatin assembly during DNA replication in vitro".
478:"DNA-mediated association of two histone-bound complexes of yeast Chromatin Assembly Factor-1 (CAF-1) drives tetrasome assembly in the wake of DNA replication"
90:
P60 interacts with ASF1a/b, which is a histone chaperone for H3/H4. p48 has roles outside of CAF-1, but when involved with the complex, it binds to H4.
190:
675:"Mechanism of mRNA deadenylation: evidence for a molecular interplay between translation termination factor eRF3 and mRNA deadenylases"
86:(proliferating cell nuclear antigen, which stabilizes CAF-1 at replication forks, is important for CAF-1's role in nucleosome assembly
1038:
527:
Zhang Z, Shibahara K, Stillman B (November 2000). "PCNA connects DNA replication to epigenetic inheritance in yeast".
427:"Insights into the molecular architecture and histone H3-H4 deposition mechanism of yeast Chromatin assembly factor 1"
180:
82:. H3 and H4 are synthesized in the cytoplasm. Several studies have shown that the interaction between CAF-1 and
1043:
1033:
123:
319:"The role of the chromatin assembly complex (CAF-1) and its p60 subunit (CHAF1b) in homeostasis and disease"
376:"The Cac1 subunit of histone chaperone CAF-1 organizes CAF-1-H3/H4 architecture and tetramerizes histones"
977:"Mechanistic insights into histone deposition and nucleosome assembly by the chromatin assembly factor-1"
161:
1028:
739:
536:
262:
133:
cells) can be induced in vitro through downregulation of the chromatin-assembly activity of CAF-1 in
251:"Chromatin assembly factor 1 is essential and couples chromatin assembly to DNA replication in vivo"
134:
63:
46:(p60), and p48 subunits in humans, or Cac1, Cac2, and Cac3, respectively, in yeast— that assembles
963:
924:"Chromatin assembly factor 1 suppresses epigenetic reprogramming toward adaptive drug resistance"
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16:
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223:
186:
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Cheloufi S, Elling U, Hopfgartner B, Jung YL, Murn J, Ninova M, et al. (December 2015).
374:
Liu WH, Roemer SC, Zhou Y, Shen ZJ, Dennehey BK, Balsbaugh JL, et al. (September 2016).
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215:
79:
476:
Mattiroli F, Gu Y, Yadav T, Balsbaugh JL, Harris MR, Findlay ES, et al. (March 2017).
20:
Steps in nucleosome assembly. CAF-1 is shown in yellow interacting with the H3-H4 tetramer.
578:
Houlard M, Berlivet S, Probst AV, Quivy JP, Héry P, Almouzni G, Gérard M (November 2006).
111:
51:
35:
673:
Funakoshi Y, Doi Y, Hosoda N, Uchida N, Osawa M, Shimada I, et al. (December 2007).
950:
923:
842:
Kaufman PD (September 2015). "Want reprogramming? Cut back on the chromatin assembly!".
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792:
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540:
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1001:
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318:
149:
425:
Sauer PV, Timm J, Liu D, Sitbon D, Boeri-Erba E, Velours C, et al. (March 2017).
285:
250:
1022:
975:
Sauer PV, Gu Y, Liu WH, Mattiroli F, Panne D, Luger K, Churchill ME (November 2018).
967:
564:
219:
157:
881:"Chromatin dynamics after DNA damage: The legacy of the access-repair-restore model"
871:
834:
580:"CAF-1 is essential for heterochromatin organization in pluripotent embryonic cells"
235:
130:
119:
659:
896:
793:"Histone chaperone CAF-1: essential roles in multi-cellular organism development"
596:
334:
107:
940:
255:
Proceedings of the
National Academy of Sciences of the United States of America
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Wang Z, Wu R, Nie Q, Bouchonville KJ, Diasio RB, Offer SM (March 2021).
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690:
494:
443:
392:
115:
47:
855:
643:
548:
153:
43:
39:
70:
formation by tetramerizing and depositing newly synthesized histone
15:
323:
Biochimica et
Biophysica Acta (BBA) - Gene Regulatory Mechanisms
145:
83:
728:"The histone chaperone CAF-1 safeguards somatic cell identity"
106:CAF-1 is required for the spatial organization and
778:"Memory loss enables the production of stem cells"
144:, which should not be confused with the unrelated
148:. The CAF-1/CCR4-Not complex cooperates with the
317:Volk, Andrew; Crispino, John D. (August 2015).
791:Yu Z, Liu J, Deng WM, Jiao R (January 2015).
129:Cells resembling 2-cell-stage mouse embryos (
8:
1000:
949:
939:
904:
844:Nature Structural & Molecular Biology
816:
759:
698:
632:Nature Structural & Molecular Biology
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595:
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493:
452:
442:
401:
391:
350:
284:
274:
179:Fang, Dong; Han, Junhong (2020-11-06).
171:
140:CAF-1 forms a deadenylase complex with
54:during the S phase of the cell cycle.
928:Journal of the National Cancer Center
879:Polo SE, Almouzni G (December 2015).
118:cells, creating a cellular memory of
7:
797:Cellular and Molecular Life Sciences
312:
310:
308:
306:
304:
249:Hoek M, Stillman B (October 2003).
784:(Press release). December 9, 2015.
14:
66:that mediates the first step in
156:to shorten the poly(A) tail of
1:
62:CAF-1 functions as a histone
897:10.1016/j.dnarep.2015.09.014
597:10.1371/journal.pgen.0020181
335:10.1016/j.bbagrm.2015.05.009
220:10.1016/0092-8674(89)90398-X
182:Histone Mutations and Cancer
1060:
941:10.1016/j.jncc.2020.12.003
809:10.1007/s00018-014-1748-3
124:cellular differentiation
78:onto DNA rapidly behind
679:Genes & Development
276:10.1073/pnas.1635158100
114:domains in pluripotent
981:Nucleic Acids Research
21:
19:
135:embryonic stem cells
752:10.1038/nature15749
744:2015Natur.528..218C
691:10.1101/gad.1597707
541:2000Natur.408..221Z
495:10.7554/eLife.22799
444:10.7554/elife.23474
393:10.7554/eLife.18023
267:2003PNAS..10012183H
261:(21): 12183–12188.
185:. Springer Nature.
1039:Induced stem cells
993:10.1093/nar/gky823
22:
987:(19): 9907–9917.
856:10.1038/nsmb.3081
738:(7581): 218–224.
685:(23): 3135–3148.
644:10.1038/nsmb.3066
535:(6809): 221–225.
192:978-981-15-8104-5
80:replication forks
28:assembly factor-1
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112:heterochromatin
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52:replicating DNA
50:tetramers onto
36:protein complex
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1021:
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850:(9): 648–650.
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803:(2): 327–337.
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638:(9): 662–671.
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329:(8): 979–986.
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150:release factor
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42:(p150),
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584:PLOS Genetics
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934:(1): 15–22.
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214:(1): 15–25.
211:
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162:translation.
139:
128:
120:somatic cell
105:
96:
92:
88:
61:
38:— including
31:
24:
23:
1029:Epigenetics
891:: 114–121.
110:marking of
1023:Categories
885:DNA Repair
488:: e22799.
437:: e23474.
386:: e18023.
167:References
131:totipotent
108:epigenetic
68:nucleosome
968:234287367
565:205010657
343:0006-3002
152:eRF3 and
116:embryonic
64:chaperone
26:Chromatin
1011:30239791
960:39036786
951:11256593
915:26429064
872:33569420
864:26333710
835:18355941
827:25292338
818:11114026
770:26659182
709:18056425
652:26237512
616:17083276
557:11089978
514:28315523
463:28315525
412:27690308
361:26066981
295:14519857
236:10515064
142:CCR4-Not
58:Function
1002:6212844
906:5113751
761:4866648
740:Bibcode
700:2081979
607:1630711
537:Bibcode
505:5404915
454:5404918
403:5045291
352:4515380
263:Bibcode
228:2546672
160:during
48:histone
34:) is a
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154:PABPC1
44:Chaf1b
40:Chaf1a
964:S2CID
868:S2CID
831:S2CID
656:S2CID
561:S2CID
482:eLife
431:eLife
380:eLife
232:S2CID
102:Roles
32:CAF-1
1007:PMID
956:PMID
911:PMID
860:PMID
823:PMID
766:PMID
705:PMID
648:PMID
612:PMID
553:PMID
510:PMID
459:PMID
408:PMID
357:PMID
339:ISSN
327:1849
291:PMID
224:PMID
208:Cell
187:ISBN
158:mRNA
146:CCR4
84:PCNA
997:PMC
989:doi
946:PMC
936:doi
901:PMC
893:doi
852:doi
813:PMC
805:doi
756:PMC
748:doi
736:528
695:PMC
687:doi
640:doi
602:PMC
592:doi
545:doi
533:408
500:PMC
490:doi
449:PMC
439:doi
398:PMC
388:doi
347:PMC
331:doi
281:PMC
271:doi
259:100
216:doi
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303:^
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76:H4
72:H3
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30:(
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