Solution structure of the motile major sperm protein (MSP) of Ascaris suum - evidence for two manganese binding sites and the possible role of divalent cations in filament formation 1 1Edited by P. E. Wright

Haaf, A.; LeClaire, Lawrence L.; Roberts, Gregory; Kent, Helen M.; Roberts, Thomas M.; Stewart, Murray; Neuhaus, David

doi:10.1006/jmbi.1998.2291

Cited by 14 publications

(8 citation statements)

References 34 publications

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“…The same applies to potential MSP phosphorylation, which is predicted at four sites in D. viviparus but found to be absent in C. elegans MSP (Burke and Ward 1983;Ward 1987;Stewart et al 1998). However, MSP might be phosphorylated transiently, like speculated by Haaf et al (1998) in the case of MSP activation which is necessary for filament nucleation and elongation. A further predicted posttranslational modification of bovine lungworm MSP was Nterminal acetylation of serine3.…”

Section: Discussionmentioning

confidence: 95%

Molecular characterization and real-time PCR transcriptional analysis of Dictyocaulus viviparus major sperm proteins

2008

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Major sperm proteins (MSPs) represent a protein family occurring in nematodes only. Identification of the 3' and 5' untranslated region (UTR) completed the so far partial msp complementary DNA sequences of the bovine lungworm Dictyocaulus viviparus. The full-length transcript contains sequence tracts consistent with the Kozak and polyadenylation consensus sequence. On genomic level, three full-length sequences differing in three nucleotides were determined containing a 65-bp phase zero intron. Conceptual translation inferred two MSP isoforms due to one substitution within the 126-amino acid polypeptide. Bioinformatic analysis predicted that bovine lungworm MSP folds into an immunoglobulin-like seven-stranded beta sandwich as known for Caenorhabditis elegans and Ascaris suum. Furthermore, bovine lungworm MSP is confidentially predicted to be N-terminal-acetylated and secreted via a non-classical pathway. Quantitative real-time polymerase chain reaction analysis using ten developmental lungworm stages showed that msp is transcribed mainly in adult male parasites and in some degree in hypobiotic L5. However, marginal msp transcription was detectable in all of the investigated developmental lungworm stages.

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Section: Discussionmentioning

confidence: 95%

Molecular characterization and real-time PCR transcriptional analysis of Dictyocaulus viviparus major sperm proteins

2008

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“…Each point represents the rms variations in the position of a given C α atom inferred from NMR and X-ray data. The results for all the aligned residues of the 64 protein pairs (not shown for clarity) yield the linear regression equation <(ΔR i ) 2 > 1/2 NMR = 2.22 <(ΔR i ) 2 > 1/2 X-ray − 0.49; that is, the NMR MSP is a dimeric β protein solved by NMR (Haaf et al, 1998) and X-ray (Bullock et al, 1996). The upper two structures depict the NMR models (left) and the X-ray structure (right) (PDB ID codes 3MSP and 1MSP, respectively).…”

Section: The Gaussian Network Modelmentioning

confidence: 95%

Insights into Equilibrium Dynamics of Proteins from Comparison of NMR and X-Ray Data with Computational Predictions

et al. 2007

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For a representative set of 64 nonhomologous proteins, each containing a structure solved by NMR and X-ray crystallography, we analyzed the variations in atomic coordinates between NMR models, the temperature (B) factors measured by X-ray crystallography, and the fluctuation dynamics predicted by the Gaussian network model (GNM). The NMR and X-ray data exhibited a correlation of 0.49. The GNM results, on the other hand, yielded a correlation of 0.59 with X-ray data and a distinctively better correlation (0.75) with NMR data. The higher correlation between GNM and NMR data, compared to that between GNM and X-ray B factors, is shown to arise from the differences in the spectrum of modes accessible in solution and in the crystal environment. Mainly, large-amplitude motions sampled in solution are restricted, if not inaccessible, in the crystalline environment of X-rays. Combined GNM and NMR analysis emerges as a useful tool for assessing protein dynamics.

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“…While many proteins on the ER can recruit a small number of cytoplasmic binding partners, one pair of ER proteins recruits a wide range of partners: v esicle-associated membrane protein- a ssociated p rotein (VAP)-A and VAP-B are highly homologous ∼240 a.a. proteins conserved in all eukaryotes consisting of a single transmembrane helix anchoring a cytoplasmic domain [8], [9]. VAPs are important partly because dysfunction of VAP-B causes motor neuron disease [10], with one proposed mechanism being that lack of VAP-B causes ER stress [11], [12], [13].…”

Section: Introductionmentioning

confidence: 99%

Analysis of the Key Elements of FFAT-Like Motifs Identifies New Proteins That Potentially Bind VAP on the ER, Including Two AKAPs and FAPP2

2012

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BackgroundTwo phenylalanines (FF) in an acidic tract (FFAT)-motifs were originally described as having seven elements: an acidic flanking region followed by 6 residues (EFFDA–E). Such motifs are found in several lipid transfer protein (LTP) families, and they interact with a protein on the cytosolic face of the ER called vesicle-associated membrane protein-associated protein (VAP). Mutation of which causes ER stress and motor neuron disease, making it important to determine which proteins bind VAP. Among other proteins that bind VAP, some contain FFAT-like motifs that are missing one or more of the seven elements. Defining how much variation is tolerated in FFAT-like motifs is a preliminary step prior to the identification of the full range of VAP interactors.ResultsWe used a quantifiable in vivo system that measured ER targeting in a reporter yeast strain that over-expressed VAP to study the effect of substituting different elements of FFAT-like motifs in turn. By defining FFAT-like motifs more widely than before, we found them in novel proteins the functions of which had not previously been directly linked to the ER, including: two PKA anchoring proteins, AKAP220 and AKAP110; a family of plant LTPs; and the glycolipid LTP phosphatidylinositol-four-phosphate adaptor-protein-2 (FAPP-2).ConclusionAll of the seven essential elements of a FFAT motif tolerate variation, and weak targeting to the ER via VAP is still detected if two elements are substituted. In addition to the strong FFAT motifs already known, there are additional proteins with weaker FFAT-like motifs, which might be functionally important VAP interactors.

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Solution structure of the motile major sperm protein (MSP) of Ascaris suum - evidence for two manganese binding sites and the possible role of divalent cations in filament formation 1 1Edited by P. E. Wright

Cited by 14 publications

References 34 publications

Molecular characterization and real-time PCR transcriptional analysis of Dictyocaulus viviparus major sperm proteins

Molecular characterization and real-time PCR transcriptional analysis of Dictyocaulus viviparus major sperm proteins

Insights into Equilibrium Dynamics of Proteins from Comparison of NMR and X-Ray Data with Computational Predictions

Analysis of the Key Elements of FFAT-Like Motifs Identifies New Proteins That Potentially Bind VAP on the ER, Including Two AKAPs and FAPP2

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