Reversible N epsilon-lysine acetylation regulates the activity of acyl-CoA synthetases involved in anaerobic benzoate catabolism in Rhodopseudomonas palustris.
Reversible N epsilon-lysine acetylation regulates the activity of acyl-CoA synthetases involved in anaerobic benzoate catabolism in Rhodopseudomonas palustris.
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DOI：
10.1111/j.1365-2958.2010.07127.x
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发表时间：
2010-05
影响因子：
3.6
通讯作者：
Escalante-Semerena JC
中科院分区：
文献类型：
--
作者：
Crosby HA;Heiniger EK;Harwood CS;Escalante-Semerena JC
沼泽红球藻在富含植物来源的木质素的水生环境中可利用的芳香化合物上光异养生长。苯甲酸降解是在转录水平上调控的。palustris响应缺氧和苯甲酸和/或苯甲酰-CoA（Bz-CoA）的存在。在这里，我们报告的证据表明，厌氧苯甲酸催化剂在这种细菌也在翻译后水平进行调节。在该途径中，苯甲酸通过AMP形成Bz-CoA合成酶（BadA）活化为Bz-CoA。质谱和突变分析数据表明残基Lys 512对BadA活性至关重要。Lys 512的乙酰化使BadA失活;去乙酰化使BadA再活化。同样地，4-羟基苯甲酰-CoA（HbaA）和环己烷羧基-CoA（阿利亚）合成酶也可逆地乙酰化。我们鉴定了一种在体外修饰BadA、Hba和阿利亚的乙酰转移酶。乙酰转移酶与肠道沙门氏菌鼠伤寒沙门氏菌LT 2的蛋白乙酰转移酶（Pat）同源，因此我们将其称为RpPat。RpPat还修饰了来自R.沼泽体内数据表明，至少有两个脱乙酰酶重新激活BadAAc。一种是SrtN（由srtN编码，以前称为rpa 2524），一种sirtuin型NAD+依赖性脱乙酰酶（O-乙酰基-ADP-核糖形成）;另一种脱乙酰酶是LdaA（由ldaA编码，赖氨酸脱乙酰酶A;以前称为rpa 0954），一种乙酸盐形成蛋白脱乙酰酶。LdaA在体外重新激活HbaAc和AliAAc。
Rhodopseudomonas palustris grows photoheterotrophically on aromatic compounds available in aquatic environments rich in plant-derived lignin. Benzoate degradation is regulated at the transcriptional level in R. palustris in response to anoxia and the presence of benzoate and/or benzoyl-CoA (Bz-CoA). Here, we report evidence that anaerobic benzoate catabolism in this bacterium is also regulated at the posttranslational level. In this pathway, benzoate is activated to Bz-CoA by the AMP-forming Bz-CoA synthetase (BadA) enzyme. Mass spectrometry and mutational analysis data indicate that residue Lys512 is critical to BadA activity. Acetylation of Lys512 inactivated BadA; deacetylation reactivated BadA. Likewise, 4-hydroxybenzoyl-CoA (HbaA) and cyclohexanecarboxyl-CoA (AliA) synthetases were also reversibly acetylated. We identified one acetyltransferase that modified BadA, Hba, and AliA in vitro. The acetyltransferase enzyme is homologous to the protein acetyltransferase (Pat) enzyme of Salmonella enterica sv Typhimurium LT2, thus we refer to it as RpPat. RpPat also modified acetyl-CoA (Ac-CoA) synthetase (Acs) from R. palustris. In vivo data indicate that at least two deacetylases reactivate BadAAc. One is SrtN (encoded by srtN, formerly rpa2524), a sirtuin-type NAD+-dependent deacetylase (O-acetyl-ADP-ribose-forming); the other deacetylase is LdaA (encoded by ldaA, for lysine deacetylase A; formerly rpa0954), an acetate-forming protein deacetylase. LdaA reactivated HbaAc and AliAAc in vitro.
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影响因子：
5.8
作者：
Gouet, P;Courcelle, E;Métoz, F
通讯作者：
Métoz, F
影响因子：
3.2
作者：
Gardner, Jeffrey G.;Escalante-Semerena, Jorge C.
通讯作者：
Escalante-Semerena, Jorge C.
DOI：
10.1073/pnas.94.12.6484
发表时间：
1997-06-10
影响因子：
11.1
作者：
Egland, PG;Pelletier, DA;Harwood, CS
通讯作者：
Harwood, CS
影响因子：
3.2
作者：
GIBSON, J;DISPENSA, M;HARWOOD, CS
通讯作者：
HARWOOD, CS
影响因子：
3.2
作者：
GUZMAN, LM;BELIN, D;BECKWITH, J
通讯作者：
BECKWITH, J