Identification of transmembrane helix 1 (TM1) surfaces important for EnvZ dimerisation and signal output
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- 作者：Annika Heiningera ; 1 ; heininger.annika@t-online.de" class="auth_mail" title="E-mail the corresponding author ; Rahmi Yusufb ; 1 ; rahmi.yusuf@port.ac.uk" class="auth_mail" title="E-mail the corresponding author ; Robert J. Lawrenceb ; robert.lawrence@port.ac.uk" class="auth_mail" title="E-mail the corresponding author ; Roger R. Draheimb ; c ; roger.draheim@port.ac.uk" class="auth_mail" title="E-mail the corresponding author
- 关键词：TM1 ; first transmembrane helix ; MDR ; multidrug resistance ; OM ; outer membrane ; SHK ; sensor histidine kinase ; TM2 ; second transmembrane helix ; HAMP ; domain found in histidine kinases ; adenylate cyclases ; MAP kinases and phosphatases ; CFP ; cyan fluorescent protein ; YFP ; yellow fluorescent protein ; IPTG ; isopropyl-β-thiogalactopyranoside ; NEM ; N-ethylmaleimide ; EDTA ; ethylenediaminetetraacetic acid ; SDS-PAGE ; sodium dodecyl sulphate-polyacrylamide gel electrophoresis ; ATP ; adenosine triphosphate
- 刊名：Biochimica et Biophysica Acta (BBA)-Biomembranes
- 出版年：2016
- 出版时间：August 2016
- 年：2016
- 卷：1858
- 期：8
- 页码：1868-1875
- 全文大小：851 K
文摘
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EnvZ maintains outer membrane porin balance in gram negative bacteria.
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TM1–TM1′ dimerisation interface of EnvZ identified by sulfhydryl-reactivity
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TM1 surfaces responsible for maintenance of EnvZ signal output identified
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Three distinct subregions of TM1 suggest tightly packed helices within the membrane core.