The protein network surrounding the human telomere repeat binding factors TRF1, TRF2, and POT1.
Telomere integrity (including telomere length and capping) is critical in overall genomic stability. Telomere repeat binding factors and their associated proteins play vital roles in telomere length regulation and end protection. In this study, we explore the protein network surrounding telomere repeat binding factors, TRF1, TRF2, and POT1 using dual-tag affinity purification in combination with multidimensional protein identification technology liquid chromatography--tandem mass spectrometry (MudPIT LC-MS/MS). After control subtraction and data filtering, we found that TRF2 and POT1 co-purified all six members of the telomere protein complex, while TRF1 identified five of six components at frequencies that lend evidence towards the currently accepted telomere architecture. Many of the known TRF1 or TRF2 interacting proteins were also identified. Moreover, putative associating partners identified for each of the three core components fell into functional categories such as DNA damage repair, ubiquitination, chromosome cohesion, chromatin modification/remodeling, DNA replication, cell cycle and transcription regulation, nucleotide metabolism, RNA processing, and nuclear transport. These putative protein-protein associations may participate in different biological processes at telomeres or, intriguingly, outside telomeres.
Giannone
Richard J
RJ
Biosciences Division, Oak Ridge National Laboratory, Oak Ridge, Tennessee, United States of America.
McDonald
Hayes W
HW
Hurst
Gregory B
GB
Shen
Rong-Fong
RF
Wang
Yisong
Y
Liu
Yie
Y
D002460:Cell Line; D002853:Chromatography, Liquid; D006801:Humans; D013058:Mass Spectrometry; D011485:Protein Binding; D000089804:Shelterin Complex; D034501:Telomere-Binding Proteins / Q000378:metabolism*; D035321:Telomeric Repeat Binding Protein 1 / Q000378:metabolism*; D035341:Telomeric Repeat Binding Protein 2 / Q000378:metabolism*
C440849:POT1 protein, human; D000089804:Shelterin Complex; D034501:Telomere-Binding Proteins; D035321:Telomeric Repeat Binding Protein 1; D035341:Telomeric Repeat Binding Protein 2
J Biol Chem. 2004 Dec 3;279(49):51338-42
15383534
Genes Cells. 2008 Oct;13(10):1045-59
18761675
EMBO J. 2007 Nov 28;26(23):4867-78
17962804
EMBO Rep. 2006 Jul;7(7):716-21
16799465
Cell. 1999 May 14;97(4):503-14
10338214
J Biol Chem. 2004 Oct 15;279(42):43799-804
15292264
Biochemistry. 2002 Jul 30;41(30):9333-40
12135354
Genome Biol. 2003;4(3):R22
12620107
Cancer Cell. 2008 Jul 8;14(1):68-78
18598945
Nat Struct Mol Biol. 2007 Jul;14(7):581-90
17589526
J Biol Chem. 2006 Jan 13;281(2):759-68
16275645
EMBO J. 2008 May 21;27(10):1513-24
18418389
Curr Biol. 2000 Oct 19;10(20):1299-302
11069113
Nat Cell Biol. 2009 May;11(5):616-23
19363487
EMBO Rep. 2002 Nov;3(11):1055-61
12393752
Genes Dev. 2004 Aug 1;18(15):1781-99
15289453
Nat Cell Biol. 2004 Jul;6(7):673-80
15181449
J Biol Chem. 2007 Feb 23;282(8):5101-5
17170104
Nature. 1997 Feb 20;385(6618):740-3
9034193
Proc Natl Acad Sci U S A. 2005 Oct 25;102(43):15539-44
16223874
Cell. 2006 Jul 14;126(1):63-77
16839877
Mol Cell Biol. 2000 Mar;20(5):1659-68
10669743
Curr Biol. 2006 Jul 11;16(13):1303-10
16730175
Nat Cell Biol. 2008 Feb;10(2):228-36
18157120
J Biol Chem. 2004 Jul 2;279(27):28585-91
15100233
EMBO J. 2007 Nov 14;26(22):4709-19
17948054
Nat Genet. 1997 Oct;17(2):231-5
9326950
Zhejiang Da Xue Xue Bao Yi Xue Ban. 2007 Jul;36(4):325-30
17717821
Curr Biol. 2008 Oct 14;18(19):1489-94
18818083
Nature. 2007 Feb 1;445(7127):506-10
17237768
EMBO J. 2005 Jul 20;24(14):2667-78
15973431
Curr Biol. 2008 Apr 8;18(7):496-500
18394896
Genome Biol. 2008;9(9):232
18828880
PLoS Biol. 2004 Aug;2(8):E240
15314656
Genes Dev. 2005 Sep 15;19(18):2100-10
16166375
Mol Cell Biol. 2009 Jul;29(13):3597-604
19398584
Proc Natl Acad Sci U S A. 2007 Aug 7;104(32):13068-73
17670947
Oncogene. 2005 May 5;24(20):3369-76
15735711
Nat Rev Genet. 2007 Apr;8(4):299-309
17363977
J Virol. 2003 Nov;77(22):11992-2001
14581536
Nature. 2007 Aug 30;448(7157):1068-71
17687332
Cell. 2009 Jul 10;138(1):90-103
19596237
Nat Genet. 2000 Jul;25(3):347-52
10888888
Genes Dev. 2008 Jan 15;22(2):125-40
18198332
Curr Biol. 2001 Oct 2;11(19):1512-6
11591318
Science. 2001 May 11;292(5519):1171-5
11349150
J Biol Chem. 2009 Dec 25;284(52):36083-36098
19797051
Crit Rev Biochem Mol Biol. 2009 Nov-Dec;44(6):434-46
19839711
Science. 2002 Mar 29;295(5564):2446-9
11923537
Annu Rev Genet. 2008;42:301-34
18680434
Science. 1995 Dec 8;270(5242):1663-7
7502076
Genes Dev. 2009 Sep 1;23(17):2060-75
19679647
Genes Dev. 2003 Jun 1;17(11):1328-33
12782650
Nat Genet. 2004 Jun;36(6):618-23
15133513
Nat Genet. 1997 Oct;17(2):236-9
9326951
Mol Cell. 2008 Jul 25;31(2):153-65
18657499
Curr Biol. 2004 Sep 21;14(18):1621-31
15380063
Genes Dev. 2004 Jul 15;18(14):1649-54
15231715
Mol Cell Biol. 2005 Feb;25(3):1070-80
15657433
J Proteome Res. 2002 Jan-Feb;1(1):21-6
12643522
Mol Biol Cell. 2006 Apr;17(4):1686-96
16436506
Nat Biotechnol. 1999 Jul;17(7):676-82
10404161
Cell. 1998 Feb 6;92(3):401-13
9476899
Cell. 2000 May 26;101(5):471-83
10850490
Cell. 2006 Jul 14;126(1):49-62
16839876
Mol Cell Biol. 2007 Aug;27(16):5898-909
17562870
Sci Am. 1996 Feb;274(2):92-7
8560215
Nat Genet. 2005 Feb;37(2):193-7
15665826
Mol Cell Biol. 2002 May;22(10):3474-87
11971978
Biotechniques. 2007 Sep;43(3):296, 298, 300 passim
17907572
Nature. 2007 Feb 1;445(7127):559-62
17237767
Nat Cell Biol. 2009 Jan;11(1):97-105
19060891
Science. 2004 Apr 2;304(5667):97-100
15064417
FEBS Lett. 2000 Sep 8;481(1):81-5
10984620