Human mitochondrial mTERF wraps around DNA through a left-handed superhelical tandem repeat

被引:34
作者
Jimenez-Menendez, Nereida [1 ,2 ]
Fernandez-Millan, Pablo [1 ]
Rubio-Cosials, Anna [1 ]
Arnan, Carme [1 ,2 ]
Montoya, Julio [3 ]
Jacobs, Howard T. [4 ,5 ]
Bernado, Pau [2 ]
Coll, Miquel [1 ,2 ]
Uson, Isabel [1 ,6 ]
Sola, Maria [1 ]
机构
[1] Inst Biol Mol Barcelona, Barcelona, Spain
[2] Inst Res Biomed, Barcelona, Spain
[3] Univ Zaragoza, CIBER Enfermedades Raras, Dept Bioquim & Biol Mol & Celular, Zaragoza, Spain
[4] Univ Tampere, Inst Med Technol, FIN-33101 Tampere, Finland
[5] Univ Tampere, Tampere Univ Hosp, FIN-33101 Tampere, Finland
[6] Inst Catalana Recerca & Estudis Avancats, Barcelona, Spain
基金
芬兰科学院;
关键词
TERMINATION FACTOR MTERF; STRUCTURAL-ANALYSIS; TRANSCRIPTION; RNA; RECOGNITION; PROTEIN; COMPLEX; BINDING; FAMILY;
D O I
10.1038/nsmb.1859
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
The regulation of mitochondrial DNA (mtDNA) processes is slowly being characterized at a structural level. We present here crystal structures of human mitochondrial regulator mTERF, a transcription termination factor also implicated in replication pausing, in complex with double-stranded DNA oligonucleotides containing the tRNA(UUR)(Leu) gene sequence. mTERF comprises nine left-handed helical tandem repeats that form a left-handed superhelix, the Zurdo domain.
引用
收藏
页码:891 / 893
页数:3
相关论文
共 16 条
[1]   Structural analysis of Bacillus subtilis SPP1 phage helicase loader protein G39P [J].
Bailey, S ;
Sedelnikova, SE ;
Mesa, P ;
Ayora, S ;
Waltho, JP ;
Ashcroft, AE ;
Baron, AJ ;
Alonso, JC ;
Rafferty, JB .
JOURNAL OF BIOLOGICAL CHEMISTRY, 2003, 278 (17) :15304-15312
[2]   Crystallographic analysis of the recognition of a nuclear localization signal by the nuclear import factor karyopherin α [J].
Conti, E ;
Uy, M ;
Leighton, L ;
Blobel, G ;
Kuriyan, J .
CELL, 1998, 94 (02) :193-204
[3]   The human mitochondrial transcription termination factor (mTERF) is a multizipper protein but binds to DNA as a monomer, with evidence pointing to intramolecular leucine zipper interactions [J].
FernandezSilva, P ;
MartinezAzorin, F ;
Micol, V ;
Attardi, G .
EMBO JOURNAL, 1997, 16 (05) :1066-1079
[4]   The structure of the β-catenin/E-cadherin complex and the molecular basis of diverse ligand recognition by β-catenin [J].
Huber, AH ;
Weis, WI .
CELL, 2001, 105 (03) :391-402
[5]   The mitochondrial transcription termination factor mTERF modulates replication pausing in human mitochondrial DNA [J].
Hyvaerinen, Anne K. ;
Pohjoismaeki, Jaakko L. O. ;
Reyes, Aurelio ;
Wanrooij, Sjoerd ;
Yasukawa, Takehiro ;
Karhunen, Pekka J. ;
Spelbrink, Johannes N. ;
Holt, Ian J. ;
Jacobs, Howard T. .
NUCLEIC ACIDS RESEARCH, 2007, 35 (19) :6458-6474
[6]   Structural analysis of the inactive state of the Escherichia coli DNA polymerase clamp-loader complex [J].
Kazmirski, SL ;
Podobnik, M ;
Weitze, TF ;
O'Donnelll, M ;
Kuriyan, J .
PROCEEDINGS OF THE NATIONAL ACADEMY OF SCIENCES OF THE UNITED STATES OF AMERICA, 2004, 101 (48) :16750-16755
[7]   TERMINATION OF TRANSCRIPTION IN HUMAN MITOCHONDRIA - IDENTIFICATION AND PURIFICATION OF A DNA-BINDING PROTEIN FACTOR THAT PROMOTES TERMINATION [J].
KRUSE, B ;
NARASIMHAN, N ;
ATTARDI, G .
CELL, 1989, 58 (02) :391-397
[8]   A family of putative transcription termination factors shared amongst metazoans and plants [J].
Linder, T ;
Park, CB ;
Asin-Cayuela, J ;
Pellegrini, M ;
Larsson, NG ;
Falkenberg, M ;
Samuelsson, T ;
Gustafsson, CM .
CURRENT GENETICS, 2005, 48 (04) :265-269
[9]   Termination factor-mediated DNA loop between termination and initiation sites drives mitochondrial rRNA synthesis [J].
Martin, M ;
Cho, JY ;
Cesare, AJ ;
Griffith, JD ;
Attardi, G .
CELL, 2005, 123 (07) :1227-1240
[10]   The Drosophila termination factor DmTTF regulates in vivo mitochondrial transcription [J].
Roberti, Marina ;
Bruni, Francesco ;
Polosa, Paola Loguercio ;
Gadaleta, Maria Nicola ;
Cantatore, Palmiro .
NUCLEIC ACIDS RESEARCH, 2006, 34 (07) :2109-2116