Scott M. Coyle coauthored a 2011 biochemical and structural investigation of Xrn1 with Martin Jinek and Jennifer A. Doudna. It linked Xrn1 5′-phosphate recognition with processivity, the persistence of successive cleavage events during an enzyme–substrate encounter.[ref]
The experimental evidence included degradation of labeled RNA assessed by polyacrylamide gel electrophoresis. Comparing intact substrate with shorter products helped distinguish efficient complete processing from the accumulation of intermediates.[ref]
Coupled 5′ nucleotide recognition and processivity in Xrn1-mediated mRNA decay by Martin Jinek and others. Results and Figure 3: degradation assays and intermediate products
An original bookkeeping example separates molecule disappearance from the number of cleaved bonds. Suppose a sample begins with identical chains, each nucleotides long. If every chain loses just one terminal nucleotide, none of the original full-length molecules remains, but nucleotides are still present in the shortened chains. Their loss from the full-length band does not imply complete conversion into individual nucleotides.
Conversely, a large amount of short product at one sampling time does not alone measure the reaction rate or prove that each chain stayed bound throughout processing. A time series and appropriate controls add information that a single end-point gel electrophoresis image cannot supply. These are interpretive examples, without an inferred assignment of individual experiments from Coyle's author position.
Scott M. Coyle, portrait linked from the University of Wisconsin–Madison Biotechnology Training Program
. [ref]Scott M. Coyle institutional portrait and author identity. Named Scott Coyle portrait; full-name correspondence confirmed by his own publication
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