Formation of the Spliceosomal A Complex

Stable Identifier
Reaction [binding]
Homo sapiens
Locations in the PathwayBrowser
SVG |   | PPTX  | SBGN
Click the image above or here to open this reaction in the Pathway Browser
The layout of this reaction may differ from that in the pathway view due to the constraints in pathway layout

The A complex is the first ATP-dependent complex in spliceosome assembly. U2AF recruits the U2 snRNP to bind to the branch site in the E complex in an ATP-dependent fashion, to form the A complex. The U2 snRNA base-pairs with the branch site, causing the branch-site adenosine to bulge out, which later positions it for nucleophilic attack at the 5' splice site. The A complex serves as a substrate for formation of the B complex.

Literature References
PubMed ID Title Journal Year
9731529 Mass spectrometry and EST-database searching allows characterization of the multi-protein spliceosome complex

Neubauer, G, Calvio, C, Rappsilber, J, Sleeman, J, Watson, M, Lamond, A, King, A, Mann, M, Ajuh, P

Nat. Genet. 1998
12176931 Large-scale proteomic analysis of the human spliceosome.

Lamond, AI, Mann, M, Rappsilber, J, Ryder, U

Genome Res 2002
11101529 Functional analysis of the human CDC5L complex and identification of its components by mass spectrometry

Lamond, AI, Kuster, B, Mann, M, Zomerdijk, JC, Panov, K, Ajuh, P

EMBO J. 2000
17332742 Composition and three-dimensional EM structure of double affinity-purified, human prespliceosomal A complexes

Sander, B, Will, CL, Lührmann, R, Deckert, J, Golas, MM, Dube, P, Stark, H, Urlaub, H, Behzadnia, N, Kastner, B, Hartmuth, K

EMBO J. 2007
12477934 Protein composition of human prespliceosomes isolated by a tobramycin affinity-selection method.

Hartmuth, K, Urlaub, H, Lührmann, R, Gentzel, M, Wilm, M, Vornlocher, HP, Will, CL

Proc Natl Acad Sci U S A 2002
Orthologous Events
Cite Us!