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Interplay between bacterial RNA 5'-termini deNADding protein NudC and DEAD-box RNA helicase CsdA in stress-responses

ABSTRACT: Nicotinamide adenine dinucleotide (NAD) "cap" recently discovered in bacteria could have similar functions as eukaryotic 7-methylguanine (m7G) "cap", which protects RNA 5'-terminus from degradation and mediates RNA interactions with proteins involved in its transportation, editing and translation. The only known 5'-NAD-RNA-interacting E. coli protein is Nudix superfamily hydrolase NudC which is responsible for this "cap" hydrolysis. We conducted the search for NudC-interacting proteins and discovered that in vivo and in vitro NudC interacts with RNA helicase DeaD. We also discovered using bacterial two hybrid system that N-terminal parts of both proteins are involved in this interaction, particularly the N-terminal domain and zinc finger motif of NudC and RecA1, RecA2 and dimerization domains of DeaD. Detailed investigation on the hydrolase interactome revealed NudC contacts with at least three proteins involved in formation of RNA degradosome complex, DeaD, Hfq and PNPase, under stress conditions raising the idea that NudC could also function within the RNA degradosome. On the other hand, NudC together with DeaD interacts with 70S ribosome proteins. Thus, NudC is closely related to protein synthesis in ribosomes. Finally, since at least six NudC-interacting partners are involved in cell stress response we think that the helicase could play important role by moduling the cell conditions in response to environment changes.

INSTRUMENT(S): Synapt G2 HDMS

ORGANISM(S): Escherichia Coli (ncbitaxon:562)

SUBMITTER: Algirdas Kaupinis

PROVIDER: MSV000089861 | MassIVE | Sun Jul 10 22:59:00 BST 2022

REPOSITORIES: MassIVE

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