Localization and interaction studies of the Salmonella enterica ethanolamine ammonia-lyase (EutBC), its reactivase (EutA), and the EutT corrinoid adenosyltransferase.
Localization and interaction studies of the Salmonella enterica ethanolamine ammonia-lyase (EutBC), its reactivase (EutA), and the EutT corrinoid adenosyltransferase.
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DOI：
10.1111/mmi.14962
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发表时间：
2022-09
影响因子：
3.6
通讯作者：
Escalante-Semerena, Jorge C.
中科院分区：
文献类型：
--
作者：
Costa, Flavia G.;Escalante-Semerena, Jorge C.
关键词：
一些原核生物区分选择的代谢能力。肠道沙门氏菌亚种肠血清型鼠伤寒沙门氏菌LT2（以下简称鼠伤寒沙门氏菌）在我们称为乙醇胺利用代谢体的蛋白质隔室内分解乙醇胺（EA）。EA分解代谢是由腺苷钴胺素（AdoCbl）依赖的乙醇胺解氨酶（EAL）启动的，该酶通过腺苷自由基机制脱氨EA，产生乙醛和氨。这种腺苷自由基可以被淬灭，需要用atp依赖的EutA再激活酶替代AdoCbl。在乙醇胺的生长过程中，鼠伤寒沙门氏菌利用ATP:Co(I)类酪氨酸腺苷转移酶（ACAT） EutT从钴胺素（Cbl）合成AdoCbl。众所周知，EAL定位于代谢体，然而，在这项工作之前，尚不清楚EutA和EutT定位于何处，以及它们是否与EAL相互作用。在这里，我们提供的证据表明EAL、EutA和EutT定位于Eut代谢体，EutA直接与EAL相互作用。我们没有观察到EutT和EAL之间的相互作用，也没有观察到EutT和EutA/EAL复合物之间的相互作用。然而，ΔeutT突变株的生长表型表明，EutT对有效的乙醇胺分解代谢至关重要。这项工作提供了一个初步的了解AdoCbl合成和使用的动力学在Eut代谢体。乙醇胺解氨酶（EAL）利用辅酶B12 （CoB12）进行乙醇胺分解代谢途径的第一步。如果co12被氧化，EAL就失去活性。我们表明，体外和体内的证据表明，EutA再激活酶直接与代谢体内的EAL相互作用，在那里乙醇胺分解代谢发生。合成co12的EutT酶也与代谢体相互作用，但不直接与EutA-EAL复合物相互作用。
Some prokaryotes compartmentalize select metabolic capabilities. Salmonella enterica subspecies enterica serovar Typhimurium LT2 (hereafter S. Typhimurium) catabolizes ethanolamine (EA) within a proteinaceous compartment that we refer to as the ethanolamine utilization (Eut) metabolosome. EA catabolism is initiated by the adenosylcobalamin (AdoCbl)-dependent ethanolamine ammonia-lyase (EAL), which deaminates EA via an adenosyl radical mechanism to yield acetaldehyde plus ammonia. This adenosyl radical can be quenched, requiring replacement of AdoCbl by the ATP-dependent EutA reactivase. During growth on ethanolamine, S. Typhimurium synthesizes AdoCbl from cobalamin (Cbl) using the ATP:Co(I)rrinoid adenosyltransferase (ACAT) EutT. It is known that EAL localizes to the metabolosome, however, prior to this work, it was unclear where EutA and EutT localized, and whether they interacted with EAL. Here, we provide evidence that EAL, EutA, and EutT localize to the Eut metabolosome, and that EutA interacts directly with EAL. We did not observe interactions between EutT and EAL nor between EutT and the EutA/EAL complex. However, growth phenotypes of a ΔeutT mutant strain show that EutT is critical for efficient ethanolamine catabolism. This work provides a preliminary understanding of the dynamics of AdoCbl synthesis and use within the Eut metabolosome. Ethanolamine ammonia-lyase (EAL) uses coenzyme B12 (CoB12) catabolizes the first step of the ethanolamine catabolic pathway. If CoB12 is oxidized, EAL becomes inactive. We show that in vitro and in vivo evidence that the EutA reactivase directly interacts with EAL inside the metabolosome, where ethanolamine catabolism takes place. The EutT enzyme that synthesizes CoB12 also interacts with the metabolosome, but not directly with the EutA-EAL complex.
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影响因子：
64.8
作者：
Jumper J;Evans R;Pritzel A;Green T;Figurnov M;Ronneberger O;Tunyasuvunakool K;Bates R;Žídek A;Potapenko A;Bridgland A;Meyer C;Kohl SAA;Ballard AJ;Cowie A;Romera-Paredes B;Nikolov S;Jain R;Adler J;Back T;Petersen S;Reiman D;Clancy E;Zielinski M;Steinegger M;Pacholska M;Berghammer T;Bodenstein S;Silver D;Vinyals O;Senior AW;Kavukcuoglu K;Kohli P;Hassabis D
通讯作者：
Hassabis D
影响因子：
3.2
作者：
BERKOWIT.D;HUSHON, JM;AMES, BN
通讯作者：
AMES, BN
影响因子：
4.8
作者：
Jakobson, Christopher M.;Kim, Edward Y.;Tullman-Ercek, Danielle
通讯作者：
Tullman-Ercek, Danielle
影响因子：
2.9
作者：
Costa, Flavia G.;Greenhalgh, Elizabeth D.;Escalante-Semerena, Jorge C.
通讯作者：
Escalante-Semerena, Jorge C.
影响因子：
3.2
作者：
Kaval, Karan Gautam;Gebbie, Margo;Garsin, Danielle A.
通讯作者：
Garsin, Danielle A.