Proteomic analysis of acetylation in thermophilic Geobacillus kaustophilus

Dong Woo Lee; Dooil Kim; Yong Jik Lee; Jung Ae Kim; Ji Young Choi; Sunghyun Kang; Jae Gu Pan

doi:10.1002/pmic.201200072

Proteomic analysis of acetylation in thermophilic Geobacillus kaustophilus

Dong Woo Lee, Dooil Kim, Yong Jik Lee, Jung Ae Kim, Ji Young Choi, Sunghyun Kang, Jae Gu Pan

Department of Biotechnology

Research output: Contribution to journal › Article › peer-review

61 Citations (Scopus)

Abstract

Recent analysis of prokaryotic N^ε-lysine-acetylated proteins highlights the posttranslational regulation of a broad spectrum of cellular proteins. However, the exact role of acetylation remains unclear due to a lack of acetylated proteome data in prokaryotes. Here, we present the N^ε-lysine-acetylated proteome of gram-positive thermophilic Geobacillus kaustophilus. Affinity enrichment using acetyl-lysine-specific antibodies followed by LC-MS/MS analysis revealed 253 acetylated peptides representing 114 proteins. These acetylated proteins include not only common orthologs from mesophilic Bacillus counterparts, but also unique G. kaustophilus proteins, indicating that lysine acetylation is pronounced in thermophilic bacteria. These data complement current knowledge of the bacterial acetylproteome and provide an expanded platform for better understanding of the function of acetylation in cellular metabolism.

Original language	English
Pages (from-to)	2278-2282
Number of pages	5
Journal	Proteomics
Volume	13
Issue number	15
DOIs	https://doi.org/10.1002/pmic.201200072
Publication status	Published - 2013 Aug

All Science Journal Classification (ASJC) codes

Biochemistry
Molecular Biology

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10.1002/pmic.201200072

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title = "Proteomic analysis of acetylation in thermophilic Geobacillus kaustophilus",

abstract = "Recent analysis of prokaryotic Nε-lysine-acetylated proteins highlights the posttranslational regulation of a broad spectrum of cellular proteins. However, the exact role of acetylation remains unclear due to a lack of acetylated proteome data in prokaryotes. Here, we present the Nε-lysine-acetylated proteome of gram-positive thermophilic Geobacillus kaustophilus. Affinity enrichment using acetyl-lysine-specific antibodies followed by LC-MS/MS analysis revealed 253 acetylated peptides representing 114 proteins. These acetylated proteins include not only common orthologs from mesophilic Bacillus counterparts, but also unique G. kaustophilus proteins, indicating that lysine acetylation is pronounced in thermophilic bacteria. These data complement current knowledge of the bacterial acetylproteome and provide an expanded platform for better understanding of the function of acetylation in cellular metabolism.",

author = "Lee, {Dong Woo} and Dooil Kim and Lee, {Yong Jik} and Kim, {Jung Ae} and Choi, {Ji Young} and Sunghyun Kang and Pan, {Jae Gu}",

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AU - Lee, Dong Woo

AU - Kim, Dooil

AU - Lee, Yong Jik

AU - Kim, Jung Ae

AU - Choi, Ji Young

AU - Kang, Sunghyun

AU - Pan, Jae Gu

PY - 2013/8

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N2 - Recent analysis of prokaryotic Nε-lysine-acetylated proteins highlights the posttranslational regulation of a broad spectrum of cellular proteins. However, the exact role of acetylation remains unclear due to a lack of acetylated proteome data in prokaryotes. Here, we present the Nε-lysine-acetylated proteome of gram-positive thermophilic Geobacillus kaustophilus. Affinity enrichment using acetyl-lysine-specific antibodies followed by LC-MS/MS analysis revealed 253 acetylated peptides representing 114 proteins. These acetylated proteins include not only common orthologs from mesophilic Bacillus counterparts, but also unique G. kaustophilus proteins, indicating that lysine acetylation is pronounced in thermophilic bacteria. These data complement current knowledge of the bacterial acetylproteome and provide an expanded platform for better understanding of the function of acetylation in cellular metabolism.

AB - Recent analysis of prokaryotic Nε-lysine-acetylated proteins highlights the posttranslational regulation of a broad spectrum of cellular proteins. However, the exact role of acetylation remains unclear due to a lack of acetylated proteome data in prokaryotes. Here, we present the Nε-lysine-acetylated proteome of gram-positive thermophilic Geobacillus kaustophilus. Affinity enrichment using acetyl-lysine-specific antibodies followed by LC-MS/MS analysis revealed 253 acetylated peptides representing 114 proteins. These acetylated proteins include not only common orthologs from mesophilic Bacillus counterparts, but also unique G. kaustophilus proteins, indicating that lysine acetylation is pronounced in thermophilic bacteria. These data complement current knowledge of the bacterial acetylproteome and provide an expanded platform for better understanding of the function of acetylation in cellular metabolism.

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Proteomic analysis of acetylation in thermophilic Geobacillus kaustophilus

Abstract

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