Dosage constraint of the ribosome-associated molecular chaperone drives the evolution and fates of its duplicates in bacteria

Gene duplication events presumably occur in <i>tig</i>, which encodes the ribosome-associated molecular chaperone trigger factor (TF). However, TF is singly copied in virtually every bacterium, and these exceptions with multiple TF homologs always retain only one complete copy while other homologs lack the N-terminal domain. Here, we reveal the manner and mechanism underlying the evolution and fates of TF duplicates in bacteria. We discovered that the mutation-to-loss or retention-to-sub/neofunctionalization of TF duplicates is associated with the dosage constraint of N-terminal complete TF. The dosage constraint of TF is attributed to its characteristic ribosome binding and substrate-holding activities, causing a decrease in protein productivity and profile changes in cellular proteome.

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Publication Details

Journal
mBio
Published
2024-10-07
DOI
https://doi.org/10.1128/mbio.01994-24
Citations
2
Primary Topic
RNA and protein synthesis mechanisms
Type
article
Field-Weighted Citation Impact
0.47

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article

Dosage constraint of the ribosome-associated molecular chaperone drives the evolution and fates of its duplicates in bacteria

Jianing Wang, Yue‐zhong Li, Zhuo Pan, Tian-yu Wan et al.
2 citations
mBio
RNA and protein synthesis mechanisms
0.47
article

Dosage constraint of the ribosome-associated molecular chaperone drives the evolution and fates of its duplicates in bacteria

Jianing Wang, Yue‐zhong Li, Zhuo Pan, Tian-yu Wan, Ya-jun Lai, Zhuo Li, Muhammad Qasim Hayat, Ying Cao, Han Ma, Rui-yun Chen, Wei-feng Hu, Jingjing Wang
article en
2 citations

Abstract

Gene duplication events presumably occur in <i>tig</i>, which encodes the ribosome-associated molecular chaperone trigger factor (TF). However, TF is singly copied in virtually every bacterium, and these exceptions with multiple TF homologs always retain only one complete copy while other homologs lack the N-terminal domain. Here, we reveal the manner and mechanism underlying the evolution and fates of TF duplicates in bacteria. We discovered that the mutation-to-loss or retention-to-sub/neofunctionalization of TF duplicates is associated with the dosage constraint of N-terminal complete TF. The dosage constraint of TF is attributed to its characteristic ribosome binding and substrate-holding activities, causing a decrease in protein productivity and profile changes in cellular proteome.

mBioVol. 15(11)
Shandong University (CN), City University of Hong Kong, Shenzhen Research Institute (CN), Suzhou Research Institute (CN)
Shandong University, National Natural Science Foundation of China, Natural Science Foundation of Jiangsu Province, Natural Science Foundation of Shandong Province, Basic and Applied Basic Research Foundation of Guangdong Province
Decent work and economic growth
Openalex Percentile: Top 35%
RNA and protein synthesis mechanisms
0.47
DOIOpen Access PDFOpenAlex
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