Lysine succinylation is a frequently occurring modification in prokaryotes and eukaryotes and extensively overlaps with acetylation

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Lysine succinylation is a frequently occurring modification in prokaryotes and eukaryotes and extensively overlaps with acetylation. / Weinert, Brian T; Schölz, Christian; Wagner, Sebastian A; Iesmantavicius, Vytautas; Su, Dan; Daniel, Jeremy A; Choudhary, Chuna Ram.

In: Cell Reports, Vol. 4, No. 4, 29.08.2013, p. 842-51.

Research output: Contribution to journal › Journal article › Research › peer-review

Harvard

Weinert, BT, Schölz, C, Wagner, SA, Iesmantavicius, V, Su, D, Daniel, JA & Choudhary, CR 2013, 'Lysine succinylation is a frequently occurring modification in prokaryotes and eukaryotes and extensively overlaps with acetylation', Cell Reports, vol. 4, no. 4, pp. 842-51. https://doi.org/10.1016/j.celrep.2013.07.024

APA

Weinert, B. T., Schölz, C., Wagner, S. A., Iesmantavicius, V., Su, D., Daniel, J. A., & Choudhary, C. R. (2013). Lysine succinylation is a frequently occurring modification in prokaryotes and eukaryotes and extensively overlaps with acetylation. Cell Reports, 4(4), 842-51. https://doi.org/10.1016/j.celrep.2013.07.024

Vancouver

Weinert BT, Schölz C, Wagner SA, Iesmantavicius V, Su D, Daniel JA et al. Lysine succinylation is a frequently occurring modification in prokaryotes and eukaryotes and extensively overlaps with acetylation. Cell Reports. 2013 Aug 29;4(4):842-51. https://doi.org/10.1016/j.celrep.2013.07.024

Author

Weinert, Brian T ; Schölz, Christian ; Wagner, Sebastian A ; Iesmantavicius, Vytautas ; Su, Dan ; Daniel, Jeremy A ; Choudhary, Chuna Ram. / Lysine succinylation is a frequently occurring modification in prokaryotes and eukaryotes and extensively overlaps with acetylation. In: Cell Reports. 2013 ; Vol. 4, No. 4. pp. 842-51.

Bibtex

@article{c9ac310942d04f729c6c639360a58c55,

title = "Lysine succinylation is a frequently occurring modification in prokaryotes and eukaryotes and extensively overlaps with acetylation",

abstract = "Recent studies have shown that lysines can be posttranslationally modified by various types of acylations. However, except for acetylation, very little is known about their scope and cellular distribution. We mapped thousands of succinylation sites in bacteria (E. coli), yeast (S. cerevisiae), human (HeLa) cells, and mouse liver tissue, demonstrating widespread succinylation in diverse organisms. A majority of succinylation sites in bacteria, yeast, and mouse liver were acetylated at the same position. Quantitative analysis of succinylation in yeast showed that succinylation was globally altered by growth conditions and mutations that affected succinyl-coenzyme A (succinyl-CoA) metabolism in the tricarboxylic acid cycle, indicating that succinylation levels are globally affected by succinyl-CoA concentration. We preferentially detected succinylation on abundant proteins, suggesting that succinylation occurs at a low level and that many succinylation sites remain unidentified. These data provide a systems-wide view of succinylation and its dynamic regulation and show its extensive overlap with acetylation.",

author = "Weinert, {Brian T} and Christian Sch{\"o}lz and Wagner, {Sebastian A} and Vytautas Iesmantavicius and Dan Su and Daniel, {Jeremy A} and Choudhary, {Chuna Ram}",

year = "2013",

month = aug,

day = "29",

doi = "10.1016/j.celrep.2013.07.024",

language = "English",

volume = "4",

pages = "842--51",

journal = "Cell Reports",

issn = "2211-1247",

publisher = "Cell Press",

number = "4",

}

RIS

TY - JOUR

T1 - Lysine succinylation is a frequently occurring modification in prokaryotes and eukaryotes and extensively overlaps with acetylation

AU - Weinert, Brian T

AU - Schölz, Christian

AU - Wagner, Sebastian A

AU - Iesmantavicius, Vytautas

AU - Su, Dan

AU - Daniel, Jeremy A

AU - Choudhary, Chuna Ram

PY - 2013/8/29

Y1 - 2013/8/29

N2 - Recent studies have shown that lysines can be posttranslationally modified by various types of acylations. However, except for acetylation, very little is known about their scope and cellular distribution. We mapped thousands of succinylation sites in bacteria (E. coli), yeast (S. cerevisiae), human (HeLa) cells, and mouse liver tissue, demonstrating widespread succinylation in diverse organisms. A majority of succinylation sites in bacteria, yeast, and mouse liver were acetylated at the same position. Quantitative analysis of succinylation in yeast showed that succinylation was globally altered by growth conditions and mutations that affected succinyl-coenzyme A (succinyl-CoA) metabolism in the tricarboxylic acid cycle, indicating that succinylation levels are globally affected by succinyl-CoA concentration. We preferentially detected succinylation on abundant proteins, suggesting that succinylation occurs at a low level and that many succinylation sites remain unidentified. These data provide a systems-wide view of succinylation and its dynamic regulation and show its extensive overlap with acetylation.

AB - Recent studies have shown that lysines can be posttranslationally modified by various types of acylations. However, except for acetylation, very little is known about their scope and cellular distribution. We mapped thousands of succinylation sites in bacteria (E. coli), yeast (S. cerevisiae), human (HeLa) cells, and mouse liver tissue, demonstrating widespread succinylation in diverse organisms. A majority of succinylation sites in bacteria, yeast, and mouse liver were acetylated at the same position. Quantitative analysis of succinylation in yeast showed that succinylation was globally altered by growth conditions and mutations that affected succinyl-coenzyme A (succinyl-CoA) metabolism in the tricarboxylic acid cycle, indicating that succinylation levels are globally affected by succinyl-CoA concentration. We preferentially detected succinylation on abundant proteins, suggesting that succinylation occurs at a low level and that many succinylation sites remain unidentified. These data provide a systems-wide view of succinylation and its dynamic regulation and show its extensive overlap with acetylation.

U2 - 10.1016/j.celrep.2013.07.024

DO - 10.1016/j.celrep.2013.07.024

M3 - Journal article

C2 - 23954790

VL - 4

SP - 842

EP - 851

JO - Cell Reports

JF - Cell Reports

SN - 2211-1247

IS - 4

ER -

ID: 57431673