Single-Molecule Studies of Telomeres and Telomerase

被引:22
作者
Parks, Joseph W. [1 ,2 ]
Stone, Michael D. [1 ,3 ]
机构
[1] Univ Calif Santa Cruz, Dept Chem & Biochem, Santa Cruz, CA 95064 USA
[2] Univ Colorado, Dept Chem & Biochem, Boulder, CO 80303 USA
[3] Ctr Mol Biol RNA, Santa Cruz, CA 95064 USA
来源
ANNUAL REVIEW OF BIOPHYSICS, VOL 46 | 2017年 / 46卷
关键词
telomerase; telomere; single-molecule biophysics; G-QUADRUPLEX STRUCTURES; N-TERMINAL DOMAIN; TETRAHYMENA TELOMERASE; RNA PSEUDOKNOT; REVERSE-TRANSCRIPTASE; DYSKERATOSIS-CONGENITA; STRUCTURAL DYNAMICS; FORCE SPECTROSCOPY; MAGNETIC TWEEZERS; FOLDING DYNAMICS;
D O I
10.1146/annurev-biophys-062215-011256
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
Telomeres are specialized chromatin structures that protect chromosome ends from dangerous processing events. In most tissues, telomeres shorten with each round of cell division, placing a finite limit on cell growth. In rapidly dividing cells, including the majority of human cancers, cells bypass this growth limit through telomerase-catalyzed maintenance of telomere length. The dynamic properties of telomeres and telomerase render them difficult to study using ensemble biochemical and structural techniques. This review describes single-molecule approaches to studying how individual components of telomeres and telomerase contribute to function. Singlemolecule methods provide a window into the complex nature of telomeres and telomerase by permitting researchers to directly visualize and manipulate the individual protein, DNA, and RNA molecules required for telomere function. The work reviewed in this article highlights how single-molecule techniques have been utilized to investigate the function of telomeres and telomerase.
引用
收藏
页码:357 / 377
页数:21
相关论文
共 128 条
[51]   Direct involvement of the TEN domain at the active site of human telomerase [J].
Jurczyluk, Julie ;
Nouwens, Amanda S. ;
Holien, Jessica K. ;
Adams, Timothy E. ;
Lovrecz, George O. ;
Parker, Michael W. ;
Cohen, Scott B. ;
Bryan, Tracy M. .
NUCLEIC ACIDS RESEARCH, 2011, 39 (05) :1774-1788
[52]   Enhanced electrostatic force microscopy reveals higher-order DNA looping mediated by the telomeric protein TRF2 [J].
Kaur, Parminder ;
Wu, Dong ;
Lin, Jiangguo ;
Countryman, Preston ;
Bradford, Kira C. ;
Erie, Dorothy A. ;
Riehn, Robert ;
Opresko, Patricia L. ;
Wang, Hong .
SCIENTIFIC REPORTS, 2016, 6
[53]   Solution Structure and Dynamics of the Wild-type Pseudoknot of Human Telomerase RNA [J].
Kim, Nak-Kyoon ;
Zhang, Qa ;
Zhou, Jung ;
Theimer, Carla A. ;
Peterson, Robert D. ;
Feigon, Juli .
JOURNAL OF MOLECULAR BIOLOGY, 2008, 384 (05) :1249-1261
[54]   SPECIFIC ASSOCIATION OF HUMAN TELOMERASE ACTIVITY WITH IMMORTAL CELLS AND CANCER [J].
KIM, NW ;
PIATYSZEK, MA ;
PROWSE, KR ;
HARLEY, CB ;
WEST, MD ;
HO, PLC ;
COVIELLO, GM ;
WRIGHT, WE ;
WEINRICH, SL ;
SHAY, JW .
SCIENCE, 1994, 266 (5193) :2011-2015
[55]  
Koirala D, 2011, NAT CHEM, V3, P782, DOI [10.1038/NCHEM.1126, 10.1038/nchem.1126]
[56]   Roles for RNA in telomerase nucleotide and repeat addition processivity [J].
Lai, CK ;
Miller, MC ;
Collins, K .
MOLECULAR CELL, 2003, 11 (06) :1673-1683
[57]   Template boundary definition in Tetrahymena telomerase [J].
Lai, CK ;
Miller, MC ;
Collins, K .
GENES & DEVELOPMENT, 2002, 16 (04) :415-420
[58]   Structural diversity and extreme stability of unimolecular Oxytricha nova telomeric G-quadruplex [J].
Lee, Ja Yil ;
Yoon, Jeongmin ;
Kihm, Hyun Woo ;
Kim, D. S. .
BIOCHEMISTRY, 2008, 47 (11) :3389-3396
[59]   Dramatic effect of single-base mutation on the conformational dynamics of human telomeric G-quadruplex [J].
Lee, Ja Yil ;
Kim, D. S. .
NUCLEIC ACIDS RESEARCH, 2009, 37 (11) :3625-3634
[60]   Extreme conformational diversity in human telomeric DNA [J].
Lee, JY ;
Okumus, B ;
Kim, DS ;
Ha, TJ .
PROCEEDINGS OF THE NATIONAL ACADEMY OF SCIENCES OF THE UNITED STATES OF AMERICA, 2005, 102 (52) :18938-18943