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重新审视蛋白质分泌的早期步骤。

Reconsidering the early steps of protein secretion.

作者信息

Hall M N, Schwartz M

出版信息

Ann Microbiol (Paris). 1982 Jan;133A(1):123-7.

PMID:7041735
Abstract

We have reviewed a unique mutation affecting the hydrophilic segment of the lambda-receptor signal sequence. Considering the implications of this mutation, we have proposed a model depicting early steps of protein secretion. The salient, novel features of this model are as follows. 1) The model explicitly states that the LamB protein must initiate the export process to be synthesized. Commitment to synthesis occur subsequent to an interaction between the hydrophilic segment of the signal sequence and a membrane export site, the initial interaction between the nascent secreted protein and the membrane. Implicit in this concept is obligatory co-translational secretion of lambda receptor. 2) We suggest the existence of a "stop translation" sequence. The role of this sequence is to halt translation in order to allow sufficient time for the hydrophilic portion of the signal sequence to initiate export by interacting with a membrane receptor. 3) We suggest that at least part of the "stop translation" sequence is located down-stream from the signal sequence, after residue 15 of the mature LamB protein. 4) We further speculate, albeit in the absence of direct evidence, that the hydrophobic portion of the signal sequence may also be part of the "stop translation" sequence.

摘要

我们已研究了一种影响λ受体信号序列亲水片段的独特突变。考虑到该突变的影响,我们提出了一个描述蛋白质分泌早期步骤的模型。该模型的显著新特点如下:1)该模型明确指出,LamB蛋白必须启动输出过程才能进行合成。在信号序列的亲水片段与膜输出位点相互作用之后,即新生分泌蛋白与膜之间的初始相互作用之后,才会发生合成的决定。这一概念中隐含着λ受体的共翻译分泌是必需的。2)我们认为存在一个“停止翻译”序列。该序列的作用是停止翻译,以便有足够的时间让信号序列的亲水部分通过与膜受体相互作用启动输出。3)我们认为“停止翻译”序列的至少一部分位于信号序列下游,在成熟LamB蛋白的第15位残基之后。4)我们进一步推测,尽管缺乏直接证据,但信号序列的疏水部分也可能是“停止翻译”序列的一部分。

相似文献

1
Reconsidering the early steps of protein secretion.重新审视蛋白质分泌的早期步骤。
Ann Microbiol (Paris). 1982 Jan;133A(1):123-7.
2
Genetic approaches to study export of LamB to the outer membrane.研究LamB向外膜输出的遗传学方法。
Ann Microbiol (Paris). 1982 Jan;133A(1):115-22.
3
Genetic studies on mechanisms of protein localization in Escherichia coli K-12.大肠杆菌K-12中蛋白质定位机制的遗传学研究。
J Supramol Struct. 1980;13(2):147-63. doi: 10.1002/jss.400130203.
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Further genetic analysis of the C-terminal external loop region in Escherichia coli maltoporin.大肠杆菌麦芽糖孔蛋白C末端外环区域的进一步基因分析。
Res Microbiol. 1997 Jun;148(5):375-87. doi: 10.1016/S0923-2508(97)83868-5.
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Rate constants of sugar transport through two LamB mutants of Escherichia coli: comparison with wild-type maltoporin and LamB of Salmonella typhimurium.糖通过大肠杆菌两个LamB突变体的转运速率常数:与野生型麦芽糖孔蛋白及鼠伤寒沙门氏菌LamB的比较。
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A system for genetic analysis in gene lamB: first results with lambda-resistant tight mutants.一种用于基因lamB中遗传分析的系统:λ抗性紧密突变体的初步结果。
Ann Microbiol (Paris). 1982 Jan;133A(1):9-20.
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In vitro synthesized bacterial outer membrane protein is integrated into bacterial inner membranes but translocated across microsomal membranes.
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Arrangement of bacteriophage lambda receptor protein (LamB) in the Escherichia coli cell surface.噬菌体λ受体蛋白(LamB)在大肠杆菌细胞表面的排列
Ann Microbiol (Paris). 1982 Jan;133A(1):43-7.
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Evidence for a coupling of synthesis and export of an outer membrane protein in Escherichia coli.大肠杆菌外膜蛋白合成与输出偶联的证据。
EMBO J. 1983;2(1):15-9. doi: 10.1002/j.1460-2075.1983.tb01373.x.
10
Purification and functional characterization of mutant LamB proteins.突变型LamB蛋白的纯化及功能特性分析
Ann Microbiol (Paris). 1982 Jan;133A(1):165-6.

引用本文的文献

1
Evidence for a coupling of synthesis and export of an outer membrane protein in Escherichia coli.大肠杆菌外膜蛋白合成与输出偶联的证据。
EMBO J. 1983;2(1):15-9. doi: 10.1002/j.1460-2075.1983.tb01373.x.
2
Mutations in a new gene, secB, cause defective protein localization in Escherichia coli.一个新基因secB中的突变会导致大肠杆菌中蛋白质定位缺陷。
J Bacteriol. 1983 Apr;154(1):253-60. doi: 10.1128/jb.154.1.253-260.1983.
3
Mutation that suppresses the protein export defect of the secY mutation and causes cold-sensitive growth of Escherichia coli.
J Bacteriol. 1984 Nov;160(2):696-701. doi: 10.1128/jb.160.2.696-701.1984.