Chinese Journal of Magnetic Resonance >
Structural Basis for Lin28 Specific Interaction with let-7 RNA
Received date: 2015-03-06
Revised date: 2015-05-11
Online published: 2015-06-05
Supported by
Grants from the Ministry of Science and Technology of China (2011CB966300), the National Natural Science Foundation of China (21272261, 21472229 and 21275154), and the Science and Technology Commission of Shanghai Municipality (15ZR1449300).
The let-7 miRNA (microRNA) family control many cell-fate determination genes to influence pluripotency, differentiation, and transformation. Lin28 is a specific, posttranscriptional inhibitor of let-7 biogenesis. The C-terminal Zn-knuckle domain (ZKD) of Lin28 specially interacts with a conserved GGAG or GGAG-like motif in let-7 miRNA. We here report the NMR structure of human Lin28 binding to let-7 RNA with a sequence of 5′-A–2A–1G1G2A3G4-3′,
demonstrating that the two folded domains of Lin28 ZKD recognize the region G1G2A3G4 of the RNA. All bases in bound RNA adopt anti conformation, and the backbone of RNA is bent due to Lin28 binding, consistent with the observations in the previous crystal structure, but different from those in the reported NMR structure, further confirming the structural basis for how Lin28 specially recognizes this RNA.
Key words： let-7; Lin28; Zn-knuckle; NMR; structure
LU Xiu-xiu1§ , GU Jia-qi2§ , LAN Wen-xian1 , WANG Chun-xi1 , MA Jin-biao2* , CAO Chun-yang1* . Structural Basis for Lin28 Specific Interaction with let-7 RNA[J]. Chinese Journal of Magnetic Resonance, 2015 , 32(2) : 318 -328 . DOI: 10.11938/cjmr20150214
[1] Pasquinelli A E, Reinhart B J, Slack F, et al. Conservation of the sequence and temporal expression of let-7 heterochronic regulatory RNA[J]. Nature, 2000, 408(6 808): 86－89.
[2] Johnson S M, Grosshans H, Shingara J, et al. RAS is regulated by the let-7 microRNA family[J]. Cell, 2005, 120(5): 635－647.
[3] Charles D J, Aurora E K, Giovanni S, et al. The let-7 microRNA represses cell proliferation pathways in human cells[J]. Cancer Res, 2007, 67(17): 7 713－7 722.
[4] James E T, Richard I G. How does Lin28 let-7 control development and disease[J]? Trends Cell Biol, 2012, 22(9): 474－482.
[5] Yu J, Vodyanik M A, Smuga-Otto K, et al. Induced pluripotent stem cell lines derived from human somatic cells[J]. Science, 2007, 318(5 858): 1 917－1 920.
[6] Viswanathan S R, Powers J T, Einhorn W, et al. Lin28 promotes transformation and is associated with advanced human malignancies[J]. Nat Genet, 2009, 41(7): 843－848.
[7] Peng S, Maihle N J, Huang Y, et al. Pluripotency factors Lin28 and Oct4 identify a sub-population of stem cell-like cells in ovarian cancer[J]. Oncogene, 2010, 29(14): 2 153－2 159.
[8] Permuth-Wey J, Kim D, Tsai Y Y, et al. Lin28B polymorphisms influence susceptibility to epithelial ovarian cancer[J]. Cancer Res, 2011, 71(11): 3 896－3 903.
[9] King C E, Cuatrecasas M, Castells A, et al. Lin28B promotes colon cancer progression and metastasis[J]. Cancer Res, 2011, 71(12): 4 260－4 268.
[10] Heo I, Joo C, Cho J, et al. Lin28 mediates the terminal uridylation of let-7 precursor microRNA[J]. Mol Cell, 2008, 32(2): 276－284.
[11] Heo I, Joo C, Kim Y K, et al. TUT4 in concert with Lin28 suppresses microRNA biogenesis through pre-microRNA uridylation[J]. Cell, 2009, 138(4): 696－708.
[12] Polesskaya A, Cuvellier S, Naguibneva I, et al. Lin28 binds IGF2 mRNA and participates in skeletal myogenesis by increasing translation efficiency[J]. Genes Dev, 2007, 21(9): 1 125－1 138.
[13] Thornton J E, Gregory R I. How does Lin28 let-7 control development and disease[J]? Trends Cell Biol, 2012, 22(9): 474－482.
[14] Viswanathan S R, Daley G Q. Lin28: A microRNA regulator with a macro role[J]. Cell, 2010, 140(4): 445－449.
[15] Loughlin F E, Gebert L F, Towbin, H, et al. Structural basis of pre-let-7 miRNA recognition by the zinc knuckles of pluripotency factor Lin28[J]. Nat Struct Mol Biol, 2012, 19(1): 84－89.
[16] Nam Y, Chen, C, Gregory R I, et al. Molecular basis for interaction of let-7 microRNAs with Lin28[J]. Cell, 2011, 147(5): 1 080－1 091.
[17] Bax A, Grzesiek S. Methodological advances in protein NMR[J]. Acc Chem Res, 1993, 26(4): 131－138.
[18] Clore G M, Gronenborn A. Determining the structures of large proteins and protein complexes by NMR[J]. Trends Biotechnol, 1998, 16(1): 22－34.
[19] Delaglio F, Grzesiek S, Vuister G W, et al. NMRPipe: a multidimensional spectral processing system based on UNIX pipes[J]. J Biomol NMR, 1995, 6(3): 277－293.
[20] Kuszewski J, Clore G M. Sources of and solutions to problems in the refinement of protein NMR structures against torsion angle potentials of mean force[J]. J Magn Reson, 2000, 146(2): 249－254.
[21] Cornilescu G, Delaglio F, Bax A. Protein backbone angle restraints from searching a database for chemical shift and sequence homology[J]. J Biomol NMR, 1999, 13(3): 289－302.
[22] Neuhaus D, Nakaseko Y, Schwabe J W, et al. Solution structures of two zinc-finger domains from SWI5 obtained using two-dimensional 1H nuclear magnetic resonance spectroscopy. A zinc-finger structure with a third strand of beta-sheet[J]. J Mol Biol, 1992, 228(2): 637－651.
[23] Cao C Y, Kwon K, Jiang Y L, et al. Solution structure and base perturbation studies reveal a novel mode of alkylated base recognition by 3-methyladenine DNA glycosylase I[J]. J Biol Chem, 2003, 278(48): 48 012－48 020.
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