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PDBsum entry 3j2c
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Nucleic Acids Res
41:2609-2620
(2013)
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PubMed id:
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Dissecting the in vivo assembly of the 30S ribosomal subunit reveals the role of RimM and general features of the assembly process.
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Q.Guo,
S.Goto,
Y.Chen,
B.Feng,
Y.Xu,
A.Muto,
H.Himeno,
H.Deng,
J.Lei,
N.Gao.
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ABSTRACT
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Ribosome biogenesis is a tightly regulated, multi-stepped process. The assembly
of ribosomal subunits is a central step of the complex biogenesis process,
involving nearly 30 protein factors in vivo in bacteria. Although the assembly
process has been extensively studied in vitro for over 40 years, very limited
information is known for the in vivo process and specific roles of assembly
factors. Such an example is ribosome maturation factor M (RimM), a factor
involved in the late-stage assembly of the 30S subunit. Here, we combined
quantitative mass spectrometry and cryo-electron microscopy to characterize the
in vivo 30S assembly intermediates isolated from mutant Escherichia coli strains
with genes for assembly factors deleted. Our compositional and structural data
show that the assembly of the 3'-domain of the 30S subunit is severely delayed
in these intermediates, featured with highly underrepresented 3'-domain proteins
and large conformational difference compared with the mature 30S subunit.
Further analysis indicates that RimM functions not only to promote the assembly
of a few 3'-domain proteins but also to stabilize the rRNA tertiary structure.
More importantly, this study reveals intriguing similarities and dissimilarities
between the in vitro and the in vivo assembly pathways, suggesting that they are
in general similar but with subtle differences.
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');
}
}
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