Nucleotide and Phospholipid-Dependent Control of PPXD and C-Domain Association for SecA ATPase

Ding, Haiyuan; Mukerji, Ishita; Oliver, Donald B.

doi:10.1021/bi035099b

Cited by 27 publications

(26 citation statements)

References 47 publications

(113 reference statements)

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“…Most conformational changes involved in the reaction cycle are poorly understood in terms of the structure, but it is clear that the endothermic conformational change induced by heat, signal peptides and by phospholipids 19 is the dissociation of the C-domain from the preprotein-binding domain in the main core of the SecA protomer. 6,20,21 In addition to the numerous conformational changes SecA readily undergoes a monomer-dimer equilibrium.…”

Section: Discussionmentioning

confidence: 99%

Asymmetric Binding Between SecA and SecB Two Symmetric Proteins: Implications for Function in Export

Randall

Crane

Lilly

et al. 2005

Journal of Molecular Biology

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Section: Discussionmentioning

confidence: 99%

Asymmetric Binding Between SecA and SecB Two Symmetric Proteins: Implications for Function in Export

Randall

Crane

Lilly

et al. 2005

Journal of Molecular Biology

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“…Whereas recent progress in the structural biology of Sec translocase is remarkable (3,4), we still lack full understanding of the dynamic and coordinated actions of the Sec components (5,6). Also, our knowledge about their regulation at the transcription͞translation level is limited.…”

mentioning

confidence: 99%

Translation arrest of SecM is essential for the basal and regulated expression of SecA

Murakami

Nakatogawa

Ito

2004

Proc. Natl. Acad. Sci. U.S.A.

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The SecM protein of Escherichia coli contains an arrest sequence (F 150 XXXXWIXXXXGIRAGP 166 ), which interacts with the ribosomal exit tunnel to halt translation elongation beyond Pro-166. This inhibition is reversed by active export of the nascent SecM chain. Here, we studied the physiological roles of SecM. Arrest-alleviating mutations in the arrest sequence reduced the expression of secA, a downstream gene on the same mRNA. Among such mutations, the arrest-abolishing P166A substitution mutation on the chromosomal secM gene proved lethal unless the mutant cells are complemented with excess SecA. Whereas secretion defect due either to azide addition, a secY mutation, or low temperature leads to up-regulated SecA biosynthesis, this regulation was lost by a secM mutation, which synergistically retarded growth of cells with lowered secretion activity. Finally, an arrest-alleviating rRNA mutation affecting the constricted part of the exit tunnel lowered the basal level of SecA as well as its secretion defect-induced upregulation. Thus, the arrest sequence of SecM has at least two roles in SecA translation. First, the transient elongation arrest in normal cells is required for the synthesis of SecA at levels sufficient to support cell growth. Second, the prolonged SecM elongation arrest under conditions of unfavorable protein secretion is required for the enhanced expression of SecA to cope with such conditions.

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“…Next, the DEAD motor ADP affinity is lost while the IRA2 detaches from the NBD and becomes disordered [87,109]. ADP released from the DEAD motor induces the PBD (with the trapped preprotein) conformational changes [50,109–110] and the dissociation of SecB [92]. Later, ATP binds to the empty nucleotide-binding cleft, and brings subsequent conformational changes that cause insertion of SecA along with bound pre-protein into the SecYEG channel.…”

Section: Seca Is An Atpase An Integral Membrane Protein and A Protein-mentioning

confidence: 99%

SecA: A Potential Antimicrobial Target

et al. 2015

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There is a consensus in the medical profession of the pressing need for novel antimicrobial agents due to issues related to drug resistance. In practice, solutions to this problem to a large degree lie with the identification of new and vital targets in bacteria and subsequently designing their inhibitors. We consider SecA a very promising antimicrobial target. In this review, we compile and analyze information available on SecA to show that inhibition of SecA has a multitude of consequences. Furthermore, we discuss issues critical to the design and evaluation of SecA inhibitors.

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Nucleotide and Phospholipid-Dependent Control of PPXD and C-Domain Association for SecA ATPase

Cited by 27 publications

References 47 publications

Asymmetric Binding Between SecA and SecB Two Symmetric Proteins: Implications for Function in Export

Asymmetric Binding Between SecA and SecB Two Symmetric Proteins: Implications for Function in Export

Translation arrest of SecM is essential for the basal and regulated expression of SecA

SecA: A Potential Antimicrobial Target

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