Shreya Ghosh is a joint first author, with Mihaela-Carmen Unciuleac, of a 2021 structural and biochemical study of polynucleotide phosphorylase from Mycobacterium smegmatis. The enzyme links reversible RNA end chemistry with the architecture of a ring-shaped protein trimer.[ref]
The researchers used a Titan Krios G2 transmission electron microscope with a Gatan K3 camera for cryo-electron microscopy. Their reconstruction located a terminal RNA segment and two magnesium ions in an active site, and an adenine base in the polynucleotide phosphorylase central channel.[ref]
Structure and mechanism of Mycobacterium smegmatis polynucleotide phosphorylase by Mihaela-Carmen Unciuleac and others. Results, Cryo-EM structure; Figures1 and4
A useful original interpretation test is to compare a structural map with a reaction time course. Suppose a map resolves four terminal nucleotides, while an independent assay measures conversion of a 12-nucleotide chain to an eight-nucleotide chain. The map identifies an occupied configuration; the assay establishes net shortening by four units. Neither alone establishes how long each intermediate persisted. Combining positional and functional evidence answers more than treating a structural snapshot as a movie.
The paper's joint authorship establishes a shared scientific contribution. It does not assign each instrument operation or analysis step to Ghosh individually.
Shreya Ghosh, named portrait in the Sloan Kettering Institute's Stewart Shuman laboratory profile
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