Mass spectrometric analysis reveals a cysteine bridge between residues 2 and 61 of the auxin‐binding protein 1 from <i>Zea mays</i> L

Feckler, Christian; Muster, Gerhard; Feser, Werner; Römer, Axel; Palme, Klaus

doi:10.1016/s0014-5793(01)03196-9

Cited by 12 publications

(5 citation statements)

References 24 publications

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“…The N-and C-terminal extensions of the ABP1 b-jellyroll barrel are linked together by a disul®de bond between Cys2 and Cys155 (Figure 2A). There is no disul®de between Cys2 and Cys61 as recently suggested (Feckler et al, 2001), and ABP1 has two cis-prolines, 127 and 148. There was also evidence in the electron density map for glycosylation of Asn95, with two N-acetyl glucosamine (GlcNAc) and three mannose (Manp) residues clearly visible [Manp(a1,6)±(Manp(a1,3))±Manp(b1,4)±GlcpNAc(b1,4) ±GlcpNAc(b1,N)-Asn]; there was weaker density for additional mannose residues.…”

Section: Overall Protein Fold Disul®de Arrangement and Glycosylationmentioning

confidence: 74%

“…The overall similarity of the ABP1 subunit to that of germin is confirmed; however, substantial differences are also revealed. Previous work has suggested a disulfide bridge between Cys2 and Cys61 of maize ABP1 (Feckler et al ., 2001) and, for tobacco ABP1 expressed in Escherichia coli , a disulfide involving the residue equivalent to 155 (David et al ., 2001). The crystal structure reveals the single disulfide is between Cys2 and Cys155, with the third cysteine, Cys61, buried close to the zinc‐binding site.…”

Section: Discussionmentioning

confidence: 99%

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Crystal structure of auxin-binding protein 1 in complex with auxin

Woo

Marshall²,

Bauly³

et al. 2002

The EMBO Journal

147

159

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The structure of auxin-binding protein 1 (ABP1) from maize has been determined at 1.9 A Ê resolution, revealing its auxin-binding site. The structure con®rms that ABP1 belongs to the ancient and functionally diverse germin/seed storage 7S protein superfamily. The binding pocket of ABP1 is predominantly hydrophobic with a metal ion deep inside the pocket coordinated by three histidines and a glutamate. Auxin binds within this pocket, with its carboxylate binding the zinc and its aromatic ring binding hydrophobic residues including Trp151. There is a single disul®de between Cys2 and Cys155. No conformational rearrangement of ABP1 was observed when auxin bound to the protein in the crystal, but examination of the structure reveals a possible mechanism of signal transduction.

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Section: Overall Protein Fold Disul®de Arrangement and Glycosylationmentioning

confidence: 74%

Section: Discussionmentioning

confidence: 99%

Crystal structure of auxin-binding protein 1 in complex with auxin

Woo

Marshall²,

Bauly³

et al. 2002

The EMBO Journal

147

159

View full text Add to dashboard Cite

show abstract

“…Thereby, tris -(2-carboxyethyl)-phosphine hydrochloride (TCEP), β-mercaptoethanol, dithiothreitol (DTT) or dithioerithritol (DTE) serve as reducing agents, whereas alkylation usually relies on iodoacetamide [ 172 , 174 ]. Alternatively, maleimide derivatives [ 190 , 191 ], acrylamide [ 192 ], 4-vinylpyridine [ 193 , 194 ], iodoacetic acid [ 195 , 196 ], and chloroacetamide [ 197 , 198 ] can be used as alkylation agents. It is important to keep in mind that the pH of the digestion buffer needs to be adjusted to the optima of corresponding enzymes ( Table 1 ), and its molarity needs to ensure a complete buffering of the sample.…”

Section: Part 1 Probing the Structure Of Glycated Proteins By Masmentioning

confidence: 99%

Maillard Proteomics: Opening New Pages

Soboleva

Schmidt

Vikhnina

et al. 2017

IJMS

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Protein glycation is a ubiquitous non-enzymatic post-translational modification, formed by reaction of protein amino and guanidino groups with carbonyl compounds, presumably reducing sugars and α-dicarbonyls. Resulting advanced glycation end products (AGEs) represent a highly heterogeneous group of compounds, deleterious in mammals due to their pro-inflammatory effect, and impact in pathogenesis of diabetes mellitus, Alzheimer’s disease and ageing. The body of information on the mechanisms and pathways of AGE formation, acquired during the last decades, clearly indicates a certain site-specificity of glycation. It makes characterization of individual glycation sites a critical pre-requisite for understanding in vivo mechanisms of AGE formation and developing adequate nutritional and therapeutic approaches to reduce it in humans. In this context, proteomics is the methodology of choice to address site-specific molecular changes related to protein glycation. Therefore, here we summarize the methods of Maillard proteomics, specifically focusing on the techniques providing comprehensive structural and quantitative characterization of glycated proteome. Further, we address the novel break-through areas, recently established in the field of Maillard research, i.e., in vitro models based on synthetic peptides, site-based diagnostics of metabolism-related diseases (e.g., diabetes mellitus), proteomics of anti-glycative defense, and dynamics of plant glycated proteome during ageing and response to environmental stress.

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“…The finding of a precisely localized disulfide bond within ABP1 typically indicates either an extracellular localization or a compartmented residence for the protein (Thornton 1981). Previous work provided proof for the presence of a disulfide bridge between the two cysteines located in the N-terminal and the central region of maize-ABP1 (Feckler et al 2001). However, the mutation of the cysteine residue located at C-terminal region of tobacco-ABP1 altered the folding of the protein, its capacity to interact with auxin and its activity at the plasma membrane (David et al 2001).…”

Section: Namementioning

confidence: 99%

Expression of auxin-binding protein1 during plum fruit ontogeny supports the potential role of auxin in initiating and enhancing climacteric ripening

et al. 2012

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Auxin-binding protein1 (ABP1) is an active element involved in auxin signaling and plays critical roles in auxin-mediated plant development. Here, we report the isolation and characterization of a putative sequence from Prunus salicina L., designated PslABP1. The expected protein exhibits a similar molecular structure to that of well-characterized maize-ABP1; however, PslABP1 displays more sequence polarity in the active-binding site due to substitution of some crucial amino-acid residues predicted to be involved in auxin-binding. Further, PslABP1 expression was assessed throughout fruit ontogeny to determine its role in fruit development. Comparing the expression data with the physiological aspects that characterize fruit-development stages indicates that PslABP1 up-regulation is usually associated with the signature events that are triggered in an auxin-dependent manner such as floral induction, fruit initiation, embryogenesis, and cell division and elongation. However, the diversity in PslABP1 expression profile during the ripening process of early and late plum cultivars seems to be due to the variability of endogenous auxin levels among the two cultivars, which consequently can change the levels of autocatalytic ethylene available for the fruit to co-ordinate ripening. The effect of auxin on stimulating ethylene production and in regulating PslABP1 was investigated. Our data suggest that auxin is involved in the transition of the mature green fruit into the ripening phase and in enhancing the ripening process in both auxin- and ethylene-dependent manners thereafter.

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Mass spectrometric analysis reveals a cysteine bridge between residues 2 and 61 of the auxin‐binding protein 1 from Zea mays L

Cited by 12 publications

References 24 publications

Crystal structure of auxin-binding protein 1 in complex with auxin

Crystal structure of auxin-binding protein 1 in complex with auxin

Maillard Proteomics: Opening New Pages

Expression of auxin-binding protein1 during plum fruit ontogeny supports the potential role of auxin in initiating and enhancing climacteric ripening

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