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M13前衣壳的两个疏水结构域都是启动膜插入所必需的。

Both hydrophobic domains of M13 procoat are required to initiate membrane insertion.

作者信息

Kuhn A, Kreil G, Wickner W

出版信息

EMBO J. 1986 Dec 20;5(13):3681-5. doi: 10.1002/j.1460-2075.1986.tb04699.x.

DOI:10.1002/j.1460-2075.1986.tb04699.x
PMID:3549284
原文链接:https://pmc.ncbi.nlm.nih.gov/articles/PMC1167410/
Abstract

M13 procoat protein has two hydrophobic domains, one in the leader peptide and one which anchors the mature coat protein in the membrane. Disruption of the membrane anchor region by insertion of arginyl residues does not yield periplasmic coat protein. Instead, the rate of membrane assembly is slowed greater than 100-fold (t1/2 less than 5 s for wild-type, t1/2 greater than 10 min for mutant). The hydrophobic region of mature coat protein not only functions as a membrane anchor, but has an important role in the membrane assembly process per se.

摘要

M13 前体外壳蛋白有两个疏水结构域,一个在引导肽中,另一个将成熟的外壳蛋白锚定在膜上。通过插入精氨酰残基破坏膜锚定区域不会产生周质外壳蛋白。相反,膜组装速率减慢超过100倍(野生型的半衰期小于5秒,突变体的半衰期大于10分钟)。成熟外壳蛋白的疏水区域不仅作为膜锚起作用,而且在膜组装过程本身中具有重要作用。

https://cdn.ncbi.nlm.nih.gov/pmc/blobs/cfed/1167410/c344aee66ad2/emboj00176-0272-b.jpg
https://cdn.ncbi.nlm.nih.gov/pmc/blobs/cfed/1167410/239765c49a4e/emboj00176-0270-a.jpg
https://cdn.ncbi.nlm.nih.gov/pmc/blobs/cfed/1167410/0d8dd93020c1/emboj00176-0271-a.jpg
https://cdn.ncbi.nlm.nih.gov/pmc/blobs/cfed/1167410/c6008797f378/emboj00176-0272-a.jpg
https://cdn.ncbi.nlm.nih.gov/pmc/blobs/cfed/1167410/c344aee66ad2/emboj00176-0272-b.jpg
https://cdn.ncbi.nlm.nih.gov/pmc/blobs/cfed/1167410/239765c49a4e/emboj00176-0270-a.jpg
https://cdn.ncbi.nlm.nih.gov/pmc/blobs/cfed/1167410/0d8dd93020c1/emboj00176-0271-a.jpg
https://cdn.ncbi.nlm.nih.gov/pmc/blobs/cfed/1167410/c6008797f378/emboj00176-0272-a.jpg
https://cdn.ncbi.nlm.nih.gov/pmc/blobs/cfed/1167410/c344aee66ad2/emboj00176-0272-b.jpg

相似文献

1
Both hydrophobic domains of M13 procoat are required to initiate membrane insertion.M13前衣壳的两个疏水结构域都是启动膜插入所必需的。
EMBO J. 1986 Dec 20;5(13):3681-5. doi: 10.1002/j.1460-2075.1986.tb04699.x.
2
The cytoplasmic carboxy terminus of M13 procoat is required for the membrane insertion of its central domain.M13原衣壳蛋白的细胞质羧基末端是其中心结构域插入膜所必需的。
Nature. 1986;322(6077):335-9. doi: 10.1038/322335a0.
3
Efficient translocation of positively charged residues of M13 procoat protein across the membrane excludes electrophoresis as the primary force for membrane insertion.
EMBO J. 1990 Aug;9(8):2385-9. doi: 10.1002/j.1460-2075.1990.tb07413.x.
4
Thermodynamics of the membrane insertion process of the M13 procoat protein, a lipid bilayer traversing protein containing a leader sequence.M13前衣壳蛋白的膜插入过程的热力学,M13前衣壳蛋白是一种含有前导序列的跨脂质双层蛋白。
Biochemistry. 1996 Jan 30;35(4):1232-41. doi: 10.1021/bi951087h.
5
Use of site-directed mutagenesis to define the limits of sequence variation tolerated for processing of the M13 procoat protein by the Escherichia coli leader peptidase.利用定点诱变确定大肠杆菌前导肽酶加工M13前衣壳蛋白所耐受的序列变异限度。
Biochemistry. 1991 Dec 24;30(51):11775-81. doi: 10.1021/bi00115a006.
6
Reconstitution of rapid and asymmetric assembly of M13 procoat protein into liposomes which have bacterial leader peptidase.M13前衣壳蛋白快速不对称组装到含有细菌前导肽酶的脂质体中。
J Biol Chem. 1983 Feb 10;258(3):1895-900.
7
Recombinant forms of M13 procoat with an OmpA leader sequence or a large carboxy-terminal extension retain their independence of secY function.带有OmpA前导序列或大型羧基末端延伸的M13原衣壳重组形式保持其对secY功能的独立性。
EMBO J. 1987 Feb;6(2):501-5. doi: 10.1002/j.1460-2075.1987.tb04781.x.
8
Bacteriophage M13 procoat protein inserts into the plasma membrane as a loop structure.噬菌体M13原衣壳蛋白以环状结构插入质膜。
Science. 1987 Dec 4;238(4832):1413-5. doi: 10.1126/science.3317833.
9
The purification of M13 procoat, a membrane protein precursor.M13前衣壳蛋白(一种膜蛋白前体)的纯化
EMBO J. 1982;1(5):573-8. doi: 10.1002/j.1460-2075.1982.tb01210.x.
10
The function of a leader peptide in translocating charged amino acyl residues across a membrane.前导肽在跨膜转运带电荷的氨酰基残基中的作用。
Science. 1990 Dec 7;250(4986):1418-21. doi: 10.1126/science.2124001.

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Front Mol Biosci. 2021 Apr 13;8:669376. doi: 10.3389/fmolb.2021.669376. eCollection 2021.
2
Targeting and Insertion of Membrane Proteins.膜蛋白的靶向与插入
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本文引用的文献

1
The spontaneous insertion of proteins into and across membranes: the helical hairpin hypothesis.蛋白质自发插入和穿过膜:螺旋发夹假说。
Cell. 1981 Feb;23(2):411-22. doi: 10.1016/0092-8674(81)90136-7.
2
The biosynthesis of membrane-bound M13 coat protein. Energetics and assembly intermediates.膜结合型M13外壳蛋白的生物合成。能量学与组装中间体。
J Biol Chem. 1982 Jun 10;257(11):6529-36.
3
The orientation of the major coat protein of bacteriophage f1 in the cytoplasmic membrane of Escherichia coli.噬菌体f1主要外壳蛋白在大肠杆菌细胞质膜中的定位
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Mechanism and hydrophobic forces driving membrane protein insertion of subunit II of cytochrome bo 3 oxidase.细胞色素bo 3氧化酶亚基II膜蛋白插入的机制及疏水作用力
J Mol Biol. 2008 Feb 1;375(5):1282-92. doi: 10.1016/j.jmb.2007.11.054. Epub 2007 Nov 22.
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Differential use of the signal recognition particle translocase targeting pathway for inner membrane protein assembly in Escherichia coli.大肠杆菌内膜蛋白组装中信号识别颗粒转位酶靶向途径的差异利用
Proc Natl Acad Sci U S A. 1998 Dec 8;95(25):14646-51. doi: 10.1073/pnas.95.25.14646.
6
In vivo membrane assembly of the E.coli polytopic protein, melibiose permease, occurs via a Sec-independent process which requires the protonmotive force.大肠杆菌多聚体蛋白蜜二糖通透酶的体内膜组装通过一种不依赖Sec的过程发生,该过程需要质子动力。
EMBO J. 1996 Oct 1;15(19):5202-8.
7
Recombinant forms of M13 procoat with an OmpA leader sequence or a large carboxy-terminal extension retain their independence of secY function.带有OmpA前导序列或大型羧基末端延伸的M13原衣壳重组形式保持其对secY功能的独立性。
EMBO J. 1987 Feb;6(2):501-5. doi: 10.1002/j.1460-2075.1987.tb04781.x.
8
Import of honeybee prepromelittin into the endoplasmic reticulum: structural basis for independence of SRP and docking protein.蜜蜂前原蜂毒肽向内质网的导入:信号识别颗粒(SRP)和对接蛋白独立性的结构基础。
EMBO J. 1987 Jul;6(7):2099-107. doi: 10.1002/j.1460-2075.1987.tb02476.x.
9
Temperature-dependent insertion of prolipoprotein into Escherichia coli membrane vesicles and requirements for ATP, soluble factors, and functional SecY protein for the overall translocation process.
J Bacteriol. 1989 Apr;171(4):1987-97. doi: 10.1128/jb.171.4.1987-1997.1989.
10
Specific recognition of the leader region of precursor proteins is required for the activation of translocation ATPase of Escherichia coli.激活大肠杆菌转位ATP酶需要对前体蛋白的前导区进行特异性识别。
Proc Natl Acad Sci U S A. 1989 Nov;86(22):8630-4. doi: 10.1073/pnas.86.22.8630.
J Biol Chem. 1981 Oct 10;256(19):9951-8.
4
A mutation downstream from the signal peptidase cleavage site affects cleavage but not membrane insertion of phage coat protein.信号肽酶切割位点下游的突变影响切割,但不影响噬菌体外壳蛋白的膜插入。
Proc Natl Acad Sci U S A. 1981 Mar;78(3):1717-21. doi: 10.1073/pnas.78.3.1717.
5
Procoat, the precursor of M13 coat protein, requires an electrochemical potential for membrane insertion.Procoat是M13外壳蛋白的前体,其插入膜中需要电化学势。
Proc Natl Acad Sci U S A. 1980 Aug;77(8):4669-73. doi: 10.1073/pnas.77.8.4669.
6
Synthesis, assembly into the cytoplasmic membrane, and proteolytic processing of the precursor of coliphage M13 coat protein.大肠杆菌噬菌体M13外壳蛋白前体的合成、组装到细胞质膜以及蛋白水解加工
J Biol Chem. 1980 Mar 10;255(5):2123-30.
7
Intracellular protein topogenesis.细胞内蛋白质拓扑结构生成
Proc Natl Acad Sci U S A. 1980 Mar;77(3):1496-500. doi: 10.1073/pnas.77.3.1496.
8
Mechanisms of membrane assembly: effects of energy poisons on the conversion of soluble M13 coliphage procoat to membrane-bound coat protein.膜组装机制:能量毒物对可溶性M13噬菌体原衣壳转化为膜结合衣壳蛋白的影响。
Proc Natl Acad Sci U S A. 1980 Feb;77(2):827-31. doi: 10.1073/pnas.77.2.827.
9
Patterns of amino acids near signal-sequence cleavage sites.信号序列切割位点附近的氨基酸模式。
Eur J Biochem. 1983 Jun 1;133(1):17-21. doi: 10.1111/j.1432-1033.1983.tb07424.x.
10
A putative signal peptidase recognition site and sequence in eukaryotic and prokaryotic signal peptides.真核生物和原核生物信号肽中一个假定的信号肽酶识别位点及序列。
J Mol Biol. 1983 Jun 25;167(2):391-409. doi: 10.1016/s0022-2836(83)80341-6.