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Structures obtained at the two frozen points, plus biochemical and mutational evidence, reveal that SUMO is adenylated by E1 while in an "open" conformation.
It is known that an adenylated substrate, bound to an E1 enzyme's adenylation site, forms a thioester link with a key cysteine at its other site, the Cys domain.
E1-SUMO Interaction E1 (pink and blue) converts from its open to its closed state and then back again as it catalyzes thioesterification of SUMO (yellow) in an adenylated form, which releases an adenine monophosphate group.
NAIPfull transcripts in this tissue could be aberrantly poly-adenylated.
Single-stranded poly-adenylated RNA standards were generated for
Poly-adenylated RNAs were amplified in the presence of aminoallyl-UTP with Amino Allyl MessageAmp II aRNA kit (Ambion).
Priming the reverse reaction with oligo-dT indicates that transcripts generated upstream of Ccl5 are poly-adenylated (