Interpretation of anomalously long crosslinks in ribosome crosslinking reveals the ribosome interaction in stationary phase E. coli.

ABSTRACT: Crosslinking mass spectrometry (XL-MS) of bacterial ribosomes revealed the dynamic intra- and intermolecular interactions within the ribosome structure. It has been also extended to capture the interactions of ribosome binding proteins during translation. Generally, XL-MS often identified the crosslinks within a cross-linkable distance (<40 Å) using amine-reactive crosslinkers. The crosslinks larger than cross-linkable distance (>40 Å) are always difficult to interpret and remain unnoticed. Here, we focused on stationary phase bacterial ribosome crosslinking that yields ultra-long crosslinks in an E. coli cell lysate. We explain these ultra-long crosslinks with the combination of sucrose density gradient centrifugation, chemical crosslinking, high-resolution mass spectrometry, and e

SUBMITTER: Misal SA 

PROVIDER: S-EPMC9257603 | biostudies-literature | 2022 Jul

REPOSITORIES: biostudies-literature