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TitleComposition and three-dimensional EM structure of double affinity-purified, human prespliceosomal A complexes.
Journal, issue, pagesEMBO J, Vol. 26, Issue 6, Page 1737-1748, Year 2007
Publish dateMar 21, 2007
AuthorsNastaran Behzadnia / Monika M Golas / Klaus Hartmuth / Bjoern Sander / Berthold Kastner / Jochen Deckert / Prakash Dube / Cindy L Will / Henning Urlaub / Holger Stark / Reinhard Lührmann /
PubMed AbstractLittle is known about the higher-order structure of prespliceosomal A complexes, in which pairing of the pre-mRNA's splice sites occurs. Here, human A complexes were isolated under physiological ...Little is known about the higher-order structure of prespliceosomal A complexes, in which pairing of the pre-mRNA's splice sites occurs. Here, human A complexes were isolated under physiological conditions by double-affinity selection. Purified complexes contained stoichiometric amounts of U1, U2 and pre-mRNA, and crosslinking studies indicated that these form concomitant base pairing interactions with one another. A complexes contained nearly all U1 and U2 proteins plus approximately 50 non-snRNP proteins. Unexpectedly, proteins of the hPrp19/CDC5 complex were also detected, even when A complexes were formed in the absence of U4/U6 snRNPs, demonstrating that they associate independent of the tri-snRNP. Double-affinity purification yielded structurally homogeneous A complexes as evidenced by electron microscopy, and allowed for the first time the generation of a three-dimensional structure. A complexes possess an asymmetric shape (approximately 260 x 200 x 195 angstroms) and contain a main body with various protruding elements, including a head-like domain and foot-like protrusions. Complexes isolated here are well suited for in vitro assembly studies to determine factor requirements for the A to B complex transition.
External linksEMBO J / PubMed:17332742 / PubMed Central
MethodsEM (single particle)
Resolution45.0 Å
Structure data

EMDB-1325:
Composition and three-dimensional EM structure of double affinity-purified, human prespliceosomal A complexes.
Method: EM (single particle) / Resolution: 45.0 Å

Source
  • Homo sapiens (human)

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