Molecular code for transmembrane-helix recognition by the Sec61 translocon

Hessa, Tara; Meindl-Beinker, Nadja M.; Bernsel, Andreas; Kim, Hyun; Sato, Yoko; Lerch-Bader, Mirjam; Nilsson, IngMarie; White, Stephen H.; Heijne, Gunnar von

doi:10.1038/nature06387

Cited by 650 publications

(1,037 citation statements)

References 29 publications

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“…The prediction of TM helices for the PNRSV MP sequence was performed using two of the most commonly used prediction methods available on the Internet: TMHMM (17) (http://www.cbs.dtu .dk/services/TMHMM-2.0/) and SOSUI (15; http://bp.nuap.nagoya-u.ac.jp /sosui/). The prediction of free-energy differences for TM helix insertion was performed using the ⌬G Prediction Server v1.0 available on the Internet (http: //www.cbr.su.se/DGpred/; 13,14). All user-adjustable parameters were left at their default values.…”

Section: Methodsmentioning

confidence: 99%

“…Nevertheless, a sequence analysis of the PNRSV MP, utilizing several algorithms (see Materials and Methods), failed to identify any membrane-spanning domain. The morehydrophobic region (residues 89 to 110) found using the ⌬G Prediction Server v1.0 (http://www.cbr.su.se/DGpred/), in which the prediction of TM helices comes from the apparent free-energy difference (⌬G app ) from insertion into ER membranes (13,14), is shown in Fig. 1A.…”

Section: Sequence Analysis Of the Pnrsv Mpmentioning

confidence: 99%

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Plant Virus Cell-to-Cell Movement Is Not Dependent on the Transmembrane Disposition of Its Movement Protein

Martínez-Gil

Sánchez‐Navarro

Cruz

et al. 2009

J Virol

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The cell-to-cell transport of plant viruses depends on one or more virus-encoded movement proteins (MPs). Some MPs are integral membrane proteins that interact with the membrane of the endoplasmic reticulum, but a detailed understanding of the interaction between MPs and biological membranes has been lacking. The cell-to-cell movement of the Prunus necrotic ringspot virus (PNRSV) is facilitated by a single MP of the 30K superfamily. Here, using a myriad of biochemical and biophysical approaches, we show that the PNRSV MP contains only one hydrophobic region (HR) that interacts with the membrane interface, as opposed to being a transmembrane protein. We also show that a proline residue located in the middle of the HR constrains the structural conformation of this region at the membrane interface, and its replacement precludes virus movement.Plant viruses encode movement proteins (MPs) that mediate the intra-and intercellular spread of the viral genome via plasmodesmata, membranous channels that traverse the walls of plant cells and enable intercellular transport and communication. There is a range of diversity in the number and type of viral proteins required for viral movement (21). Research on tobacco mosaic virus (TMV) has played a leading role in understanding MP activity (2). The genome of TMV encodes a single 30-kDa multidomain protein, the namesake of the 30K superfamily (7). Viral RNA is associated with the membrane of the endoplasmic reticulum (ER) and microtubules in the presence of this MP (23,30).A large number of plant viruses have 30K MPs, which share common abilities, including binding nucleic acids, localizing and increasing the size exclusion limit of plasmodesmata, and interacting with the ER membrane. A topological model has been proposed in which the TMV MP has two putative transmembrane (TM) helices, both the N and C termini oriented toward the cytoplasm, and a short loop exposed in the ER lumen (4). There is less experimental information for other 30K MPs, but they are likely to have some membrane interaction.Direct experimental evidence of the integration of MPs into the membrane has been obtained only for small hydrophobic MPs that do not belong to the 30K superfamily. There are two TM segments in the p9 protein of carnation mottle virus (41), whereas the p6 protein of beet yellow virus (29) and the p7B protein of melon necrotic spot virus (22) have a single TM segment. In viruses with genomes that include three partially overlapping open reading frames, termed the triple-gene block (TGB), all three TGB proteins are required for movement where the two smaller proteins, TGBp2 and TGBp3, are also TM proteins (24). Furthermore, cross-linking experiments with carnation mottle virus p9 protein demonstrated that its membrane insertion occurs cotranslationally in a signal recognition particle-dependent manner and throughout the cellular membrane integration components, the translocon (33, 34).Prunus necrotic ringspot virus (PNRSV) is a tripartite, positive-strand RNA virus in the genus Ilarvirus ...

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Section: Methodsmentioning

confidence: 99%

Section: Sequence Analysis Of the Pnrsv Mpmentioning

confidence: 99%

Plant Virus Cell-to-Cell Movement Is Not Dependent on the Transmembrane Disposition of Its Movement Protein

Martínez-Gil

Sánchez‐Navarro

Cruz

et al. 2009

J Virol

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“…24 This is in contrast to what has been observed in apolar solvents, indicating that such solvents do not accurately approximate the membrane environment. This might also explain the observed difference between the biological hydrophobicity scale 25,26 and other hydrophobicity scales, most of which were derived from experimental setups utilizing apolar solvents. In general, both experimental and theoretical studies in these solvents indicate a significantly higher energetic cost for inserting polar groups into a lipid environment than what the biological hydrophobicity scale predicts.…”

Section: Stabilizing Forces Of Membrane Proteinsmentioning

confidence: 99%

“…However, they are energetically tolerated toward the termini of the transmembrane helices. 26,36 In particular, the polar groups of the long side chains in arginine and lysine can "snorkel", that is, orient themselves so that the polar groups approach the interfacial and aqueous regions. This allows them to pull hydrating waters into the hydrocarbon part of the bilayer and create polar microenvironments for themselves.…”

Section: Amino Acid Preferences Of R-helical Membrane Proteinsmentioning

confidence: 99%

An Introduction to Membrane Proteins

2011

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R-Helical membrane proteins are important for many biological functions. Due to physicochemical constraints, the structures of membrane proteins differ from the structure of soluble proteins. Historically, membrane protein structures were assumed to be more or less two-dimensional, consisting of long, straight, membrane-spanning parallel helices packed against each other. However, during the past decade, a number of the new membrane protein structures cast doubt on this notion. Today, it is evident that the structures of many membrane proteins are equally complex as for many soluble proteins. Here, we review this development and discuss the consequences for our understanding of membrane protein biogenesis, folding, evolution, and bioinformatics.

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“…2D, middle panel). When TM5 from Mdl1p was replaced by the TM segment from Sco2p or She9p, the major product was L-MFP for the 1-5TM constructs in the Dyta10 strain, indicating that the altered The TM domains are predicted by TOPCONS [39], and the free energy of membrane insertion for each TM segment is calculated by the DG predictor [40].…”

Section: Tm5 Of Mdl1p Is Translocated Into the Matrixmentioning

confidence: 99%

Mode of membrane insertion of individual transmembrane segments in Mdl1 and Mdl2, multi‐spanning mitochondrial ABC transporters

et al. 2014

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a b s t r a c tThe sorting of an individual transmembrane (TM) segment of multi-spanning membrane proteins by the TIM23 complex in the mitochondrial inner membrane is poorly understood. Using the Mgm1 fusion approach, we attempted to assess the membrane insertion of individual TM segments of Mdl1p and Mdl2p, mitochondrial ABC transporters. Although these transporters share high sequence similarity, our results show that their membrane sorting patterns differ and that specific residues in TM domains strongly influence membrane insertion or translocation. These data imply that TIM23-mediated membrane insertion highly depends on the TM domain sequence context.

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Molecular code for transmembrane-helix recognition by the Sec61 translocon

Cited by 650 publications

References 29 publications

Plant Virus Cell-to-Cell Movement Is Not Dependent on the Transmembrane Disposition of Its Movement Protein

Plant Virus Cell-to-Cell Movement Is Not Dependent on the Transmembrane Disposition of Its Movement Protein

An Introduction to Membrane Proteins

Mode of membrane insertion of individual transmembrane segments in Mdl1 and Mdl2, multi‐spanning mitochondrial ABC transporters

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