Polymerization of the SAM domain of TEL in leukemogenesis and transcriptional repression

被引：218
作者：
Kim, CA [1 ]
Phillips, ML [1 ]
Kim, W [1 ]
Gingery, M [1 ]
Tran, HH [1 ]
Robinson, MA [1 ]
Faham, S [1 ]
Bowie, JU [1 ]
机构：
[1] Univ Calif Los Angeles, Dept Biochem & Chem, US DOE, Lab Struct Biol & Mol Med, Los Angeles, CA 90024 USA
来源：
EMBO JOURNAL | 2001年 / 20卷 / 15期
关键词：
chromatin silencing; leukemia; oncogene; Pointed domain; polycomb group proteins;
D O I：
10.1093/emboj/20.15.4173
中图分类号：
Q5 [生物化学]; Q7 [分子生物学];
学科分类号：
071010 ; 081704 ;
摘要：
TEL is a transcriptional repressor that is a frequent target of chromosomal translocations in a large number of hematalogical malignancies. These rearrangements fuse a potent oligomerization module, the SAM domain of TEL, to a variety of tyrosine kinases or transcriptional regulatory proteins. The self-associating property of TEL-SAM is essential for cell transformation in many, if not all of these diseases. Here we show that the TEL-SAM domain forms a helical, head-to-tail polymeric structure held together by strong intermolecular contacts, providing the first clear demonstration that SAM domains can polymerize. Our results also suggest a mechanism by which SAM domains could mediate the spreading of transcriptional repression complexes along the chromosome.
引用
收藏
页码：4173 / 4182
页数：10
相关论文
共 54 条
[1]   Crystal structure of the BTB domain from PLZF [J].
Ahmad, KF ;
Engel, CK ;
Privé, GG .
PROCEEDINGS OF THE NATIONAL ACADEMY OF SCIENCES OF THE UNITED STATES OF AMERICA, 1998, 95 (21) :12123-12128
[2]   THE CCP4 SUITE - PROGRAMS FOR PROTEIN CRYSTALLOGRAPHY [J].
BAILEY, S .
ACTA CRYSTALLOGRAPHICA SECTION D-BIOLOGICAL CRYSTALLOGRAPHY, 1994, 50 :760-763
[3]   Mae mediates MAP kinase phosphorylation of Ets transcription factors in Drosophila [J].
Baker, DA ;
Mille-Baker, B ;
Wainwright, SM ;
Ish-Horowicz, D ;
Dibb, NJ .
NATURE, 2001, 411 (6835) :330-334
[4]   Crystallography & NMR system:: A new software suite for macromolecular structure determination [J].
Brunger, AT ;
Adams, PD ;
Clore, GM ;
DeLano, WL ;
Gros, P ;
Grosse-Kunstleve, RW ;
Jiang, JS ;
Kuszewski, J ;
Nilges, M ;
Pannu, NS ;
Read, RJ ;
Rice, LM ;
Simonson, T ;
Warren, GL .
ACTA CRYSTALLOGRAPHICA SECTION D-BIOLOGICAL CRYSTALLOGRAPHY, 1998, 54 :905-921
[5]   The MN1-TEL fusion protein, encoded by the translocation (12;22)(p13;q11) in myeloid leukemia, is a transcription factor with transforming activity [J].
Buijs, A ;
van Rompaey, L ;
Molijn, AC ;
Davis, JN ;
Vertegaal, ACO ;
Potter, MD ;
Adams, C ;
van Baal, S ;
Zwarthoff, EC ;
Roussel, MF ;
Grosveld, GC .
MOLECULAR AND CELLULAR BIOLOGY, 2000, 20 (24) :9281-9293
[6]   The TEL platelet-derived growth factor beta receptor (PDGF beta R) fusion in chronic myelomonocytic leukemia is a transforming protein that self-associates and activates PDGF beta R kinase-dependent signaling pathways [J].
Carroll, M ;
Tomasson, MH ;
Barker, GF ;
Golub, TR ;
Gilliland, DG .
PROCEEDINGS OF THE NATIONAL ACADEMY OF SCIENCES OF THE UNITED STATES OF AMERICA, 1996, 93 (25) :14845-14850
[7]   The leukemia-associated gene TEL encodes a transcription repressor which associates with SMRT and mSin3A [J].
Chakrabarti, SR ;
Nucifora, G .
BIOCHEMICAL AND BIOPHYSICAL RESEARCH COMMUNICATIONS, 1999, 264 (03) :871-877
[8]   Solution structure of a conserved C-terminal domain of p73 with structural homology to the SAM domain [J].
Chi, SW ;
Ayed, A ;
Arrowsmith, CH .
EMBO JOURNAL, 1999, 18 (16) :4438-4445
[9]   Cell surface receptors [J].
Deller, MC ;
Jones, EY .
CURRENT OPINION IN STRUCTURAL BIOLOGY, 2000, 10 (02) :213-219
[10]   Fusion of ETV6 to neurotrophin-3 receptor TRKC in acute myeloid leukemia with t(12;15)(p13;q25) [J].
Eguchi, M ;
Eguchi-Ishimae, M ;
Tojo, A ;
Morishita, K ;
Suzuki, K ;
Sato, Y ;
Kudoh, S ;
Tanaka, K ;
Setoyama, M ;
Nagamura, F ;
Asano, S ;
Kamada, N .
BLOOD, 1999, 93 (04) :1355-1363
123456