Structure, Dynamics and Folding of an Immunoglobulin Domain of the Gelation Factor (ABP-120) from Dictyostelium discoideum

被引:28
作者
Hsu, Shang-Te Danny [1 ]
Cabrita, Lisa D. [1 ,2 ,3 ]
Fucini, Paola [4 ,5 ]
Dobson, Christopher M. [1 ]
Christodoulou, John [1 ,2 ,3 ]
机构
[1] Univ Cambridge, Dept Chem, Cambridge CB2 1EW, England
[2] UCL, Inst Struct & Mol Biol, London, England
[3] Univ London Birkbeck Coll, Sch Crystallog, London WC1E 6TB, England
[4] Max Planck Inst Mol Genet, AG Ribosome, D-14195 Berlin, Germany
[5] Goethe Univ Frankfurt, Inst Organ Chem & Chem Biol, D-60438 Frankfurt, Germany
关键词
NMR spectroscopy; co-translational folding; diffusion anisotropy; urea denaturation; filamin; A ABP-280 MOLECULES; ROTATIONAL DIFFUSION; CRYSTAL-STRUCTURE; NMR RELAXATION; ACTIN-BINDING; FILAMIN; CELL; RECOGNITION; PREDICTION; ALIGNMENT;
D O I
10.1016/j.jmb.2009.02.063
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
We have carried out a detailed structural and dynamical characterisation of the isolated fifth repeat of the gelation factor (ABP-120) from Dictyostelium discoideum (ddFLN5) by NMR spectroscopy to provide a basis for studies of co-translational folding on the ribosome of this immunoglobulin-like domain. The isolated ddFLN5 call fold autonomously ill Solution into a structure that resembles very closely the crystal structure of the domain in a construct in which the adjacent sixth repeat (ddFLN6) is covalently linked to its C-terminus in tandem but deviates locally from a second crystal Structure in which ddFLN5 is flanked by ddFLN4 and ddFLN6 at both N- and C-terminal. Conformational fluctuations were observed via N-15 relaxation methods and are primarily localised in the interstrand loops that encompass the C-terminal hemisphere. These fluctuations are distinct in location from the region where line broadening is observed in ddFLN5 when attached to the ribosome as part of a nascent chain. This observation Supports the conclusion that the broadening is associated with interactions with the ribosome surface [Hsu, S. T. D., Fucini, P., Cabrita, L D., Launay H., Dobson, C. M. & Christodoulou, J. (2007). Structure and dynamics of a ribosome-bound nascent chain by NMR spectroscopy. Proc. Natl. Acad. Sci. USA, 104, 16516-16521]. The unfolding of ddFLN5 induced by high concentrations of urea shows a low population of a folding intermediate, as inferred from all intensity-based analysis, a finding that differs from that of ddFLN5 as a ribosome-bound nascent chain. These results Suggest that interesting differences in detail may exist between the structure of the domain in isolation and when linked to the ribosome and between protein folding in vitro and the folding of a nascent chain as it emerges from the ribosome. (C) 2009 Published by Elsevier Ltd.
引用
收藏
页码:865 / 879
页数:15
相关论文
共 43 条
[11]   BACKBONE DYNAMICS OF A FREE AND A PHOSPHOPEPTIDE-COMPLEXED SRC HOMOLOGY-2 DOMAIN STUDIED BY N-15 NMR RELAXATION [J].
FARROW, NA ;
MUHANDIRAM, R ;
SINGER, AU ;
PASCAL, SM ;
KAY, CM ;
GISH, G ;
SHOELSON, SE ;
PAWSON, T ;
FORMANKAY, JD ;
KAY, LE .
BIOCHEMISTRY, 1994, 33 (19) :5984-6003
[12]   The many faces of filamin: A versatile molecular scaffold for cell motility and signalling [J].
Feng, YY ;
Walsh, CA .
NATURE CELL BIOLOGY, 2004, 6 (11) :1034-1038
[13]   The repeating segments of the F-actin cross-linking gelation factor (ABP-120) have an immunoglobulin-like fold [J].
Fucini, P ;
Renner, C ;
Herberhold, C ;
Noegel, AA ;
Holak, TA .
NATURE STRUCTURAL BIOLOGY, 1997, 4 (03) :223-230
[14]   Mechanical unfolding of single filamin A (ABP-280) molecules detected by atomic force microscopy [J].
Furuike, S ;
Ito, T ;
Yamazaki, M .
FEBS LETTERS, 2001, 498 (01) :72-75
[15]   An NMR view of the folding process of a CheY mutant at the residue level [J].
Garcia, P ;
Serrano, L ;
Rico, M ;
Bruix, M .
STRUCTURE, 2002, 10 (09) :1173-1185
[16]   Three-dimensional structures of translating ribosomes by cryo-EM [J].
Gilbert, RJC ;
Fucini, P ;
Connell, S ;
Fuller, SD ;
Nierhaus, KH ;
Robinson, CV ;
Dobson, CM ;
Stuart, DI .
MOLECULAR CELL, 2004, 14 (01) :57-66
[17]  
Goddard T.D, SPARKY 3
[18]   The folding and evolution of multidomain proteins [J].
Han, Jung-Hoon ;
Batey, Sarah ;
Nickson, Adrian A. ;
Teichmann, Sarah A. ;
Clarke, Jane .
NATURE REVIEWS MOLECULAR CELL BIOLOGY, 2007, 8 (04) :319-330
[19]  
Hardesty Boyd, 1999, Current Opinion in Structural Biology, V9, P111, DOI 10.1016/S0959-440X(99)80014-1
[20]   Dynamics and metal exchange properties of C4C4 RING domains from CNOT4 and the p44 subunit of TFIIH [J].
Houben, K ;
Wasielewski, E ;
Dominguez, C ;
Kellenberger, E ;
Atkinson, RA ;
Timmers, HTM ;
Kieffer, B ;
Boelens, R .
JOURNAL OF MOLECULAR BIOLOGY, 2005, 349 (03) :621-637