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Dynamic enzyme docking to the ribosome coordinates N-terminal processing with polypeptide folding.

Abstract：

:Newly synthesized polypeptides undergo various cotranslational maturation steps, including N-terminal enzymatic processing, chaperone-assisted folding and membrane targeting, but the spatial and temporal coordination of these steps is unclear. We show that Escherichia coli methionine aminopeptidase (MAP) associates with ribosomes through a charged loop that is crucial for nascent-chain processing and cell viability. MAP competes with peptide deformylase (PDF), the first enzyme to act on nascent chains, for binding sites at the ribosomal tunnel exit. PDF has extremely fast association and dissociation kinetics, which allows it to frequently sample ribosomes and ensure the processing of nascent chains after their emergence. Premature recruitment of the chaperone trigger factor, or polypeptide folding, negatively affect processing efficiency. Thus, the fast ribosome association kinetics of PDF and MAP are crucial for the temporal separation of nascent-chain processing from later maturation events, including chaperone recruitment and folding.

journal_name

Nat Struct Mol Biol

journal_title

Nature structural & molecular biology

authors

Sandikci A,Gloge F,Martinez M,Mayer MP,Wade R,Bukau B,Kramer G

doi

10.1038/nsmb.2615

subject

Has Abstract

pub_date

2013-07-01 00:00:00

pages

843-50

issue

7

eissn

1545-9993

issn

1545-9985

pii

nsmb.2615

journal_volume

20

pub_type

杂志文章

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