Novel Fold Revealed by the Structure of a FAS1 Domain Pair from the Insect Cell Adhesion Molecule Fasciclin I

Clout, Naomi J.; Tisi, Dominic; Hohenester, Erhard

doi:10.1016/s0969-2126(03)00002-9

Cited by 100 publications

(99 citation statements)

References 26 publications

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“…Because no crystal structures of FLA4 or FEI RLKs are available, we approached this question using molecular modelling. One of the crystal structures of Fas1 domains in the Protein Data Bank belongs to human transforming growth factor-beta-induced protein (TGFBIp) having four Fas1 domains (PDB ID 5NV6, 10 ) and another one shows the Fas1-3 and Fas1-4 domains of Drosophila fasciclin I (PDB ID 1O70, 11 ). We used SwissModel to make a homology model of FLA4 using these two crystal structures as a template.…”

Section: Resultsmentioning

confidence: 99%

A speculation on the tandem fasciclin 1 repeat of FLA4 proteins in angiosperms

Turupcu

Almohamed

Oostenbrink

et al. 2018

Plant Signaling & Behavior

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The Arabidopsis thaliana Fasciclin like arabinogalactan protein 4 (FLA4) locus is required for normal root growth in a linear genetic pathway with the FEI1 and FEI2 loci coding for receptor-like kinases. The two Fas1 domains of FLA4 are conserved among angiosperms but only the C-terminal Fas1 domain is required for genetic function. We show that at low salt deletion of the N-terminal Fas1 domain of transgenic FLA4 leads to enhanced root elongation compared to the tandem Fas1 wild type version. Modeling the hypothetical interaction between FLA4 and FEI1 we show that the predicted interaction is predominantly involving the C-terminal Fas1 domain. Relative conformational mobility between the two FLA4 Fas1 domains might regulate the interaction with the FEI receptor kinases. We therefore speculate that the FLA4 FEI complex might be a sensor for environmental conditions in the apoplast.

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Section: Resultsmentioning

confidence: 99%

A speculation on the tandem fasciclin 1 repeat of FLA4 proteins in angiosperms

Turupcu

Almohamed

Oostenbrink

et al. 2018

Plant Signaling & Behavior

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“…The L R proteins can be grouped into three classes on the basis of their structures (Extended Data Fig. 3f, g): the first class includes L R 1-L R 3 and contains the Pfam00427 domain; the second class possesses a previously unidentified, conserved chromophore-binding domain; and the third class has only one member (L R 9) and bears the FAS1 domain, which is critical for cell adhesion 29 . Figure 2 illustrates how a rod (Rb is used here) is assembled.…”

Section: Rod Linker Proteinsmentioning

confidence: 99%

“…These proteins share a similar conformation distinguished by a structural element in the middle and extensions at both sides (Extended Data Figs 3f, g, 8). The structural element comprises a long α -helix in L RC 4 and L RC 5 and a FAS1 29,33 domain in L RC 6 (Extended Data Figs 3f, g, 8). The long α -helix of L RC 4 and L RC 5 spans one α -subunit of the core trimer (Extended Data Fig.…”

Section: Rod-core Linker Proteinsmentioning

confidence: 99%

Structure of phycobilisome from the red alga Griffithsia pacifica

Zhang

Liu

et al. 2017

Nature

201

199

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The cyanobacteria and red algae are two important groups of photosynthetic organisms that share a light-harvesting antenna known as the phycobilisome (PBS) [1][2][3][4] . PBSs are among the largest protein complexes in the living world and consist of phycobiliproteins (PBPs), including phycocyanin, phycoerythrin and allophycocyanin (APC), and linker proteins . Two subunits of PBPs, the α -and β -subunits, form an α β heterodimer that is conventionally called an (α β ) monomer. The monomer is then assembled into an (α β ) 3 trimer, the basic unit of PBS hierarchical assembly. The trimers of various PBPs are organized into a highly ordered supramolecular complex with the help of the linker proteins 1,5,6 . Four morphological types of PBS 1 are known: hemidiscoidal 7 , hemiellipsoidal 8 , block-type 9 and bundle-type 10. The hemidiscoidal PBS contains a central core surrounded by peripheral rods 1,11,12 . The chromophores in hemidiscoidal PBS are arranged in such a way that a photon absorbed by a chromophore in the peripheral rods is rapidly funnelled to chromophores in the core 13 and eventually to the terminal emitters (the core-membrane linker protein (L CM ) [14][15][16] or allophycocyanin D (ApcD) 17,18 ). The terminal emitters then transfer the energy to photosynthetic reaction centres 16,[19][20][21][22][23] . Currently, the mechanism of PBS assembly is poorly understood and the energy transfer routes within PBSs are not well defined. Although 3D structures of some individual PBPs have been reported (reviewed in refs 2, 3), the structures of most linker proteins are unknown and the complete structure of a PBS has not been published, to our knowledge. Here we report the cryo-electron microscopy (cryo-EM) structure of a PBS from the red alga Griffithsia pacifica at a resolution of 3.5 Å, which reveals details of the PBS architecture. Overall structureThe PBS from G. pacifica was purified and its intactness confirmed by its protein composition and spectroscopic features (Extended Data Fig. 1a-f). We reconstructed a 3D structure of the intact PBS by single particle cryo-EM with an overall resolution of 3.5 Å (Extended Data Table 1). Applying individual local masks improved the resolutions of local maps to 3.4-4.3 Å (Extended Data Fig. 2g). The PBS is one of the largest supramolecular complexes that has been reported, with a calculated molecular mass of approximately 16.8 megadaltons. The overall appearance is block-type 9 with twofold symmetry oriented perpendicularly to the thylakoid membranes (Fig. 1a-c and Extended Data Figs 1g-l, 3a-d). This PBS is larger than the hemiellipsoidal PBS isolated from Porphyridium cruentum8 and has dimensions of approximately 680 Å length, 390 Å height, and 450 Å thickness (Fig. 1a-c).The PBS contains a triangular core with the top cylinder B (formed by two APC trimers) sitting above two basal cylinders A and A′ (each formed by three APC trimers) surrounded by peripheral rods arranged in a staggered fashion (Fig. 1a-c and Extended Data Fig. 3c-e). In addition to the core and ...

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“…The protein also appears to be involved in endothelial cell-matrix interactions during vascular remodeling and angiogenesis (21) and as a negative regulator of mineralization during cartilage differentiation and osteogenesis (22)(23)(24). Mutations in the human ␤ig-h3 gene (TGFBI) have been linked to several autosomal dominant corneal dystrophies (4) characterized by severe visual impairment resulting from the progressive accumulation of ␤ig-h3-containing protein deposits in the corneal matrix (25,26).To elucidate the function of ␤ig-h3 within the extracellular matrix, studies in our laboratory have focused on the localization, molecular forms, and matrix interactions of ␤ig-h3 within various tissues. Ultrastructural localization studies on developing tissues showed that, in most instances, ␤ig-h3 was loosely associated with collagen fibers although, in developing kidney, labeling was also observed close to the tubular and capsular basement membranes.…”

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confidence: 99%

βig-h3 Interacts Directly with Biglycan and Decorin, Promotes Collagen VI Aggregation, and Participates in Ternary Complexing with These Macromolecules

Reinboth

Thomas

Hanssen

et al. 2006

Journal of Biological Chemistry

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Recombinant human ␤ig-h3 was found to bind 125 I-labeled small leucine-rich proteoglycans (SLRPs), biglycan, and decorin, in co-immunoprecipitation experiments. In each instance the binding could be blocked by an excess of the unlabeled proteoglycan, confirming the specificity of the interaction. Scatchard analysis showed that biglycan bound ␤ig-h3 more avidly than decorin with K d values estimated as 5.88 ؋ 10 ؊8 and 1.02 ؋ 10 ؊7 M, respectively. In reciprocal blocking experiments both proteoglycans inhibited the others binding to ␤ig-h3 indicating that they may share the same binding site or that the two binding sites are in close proximity on the ␤ig-h3 molecule. Since ␤ig-h3 and the SLRPs are known to be associated with the amino-terminal region of collagen VI in tissue microfibrils, the effects of including collagen VI in the incubations were investigated. Co-immunoprecipitation of 125 I-labeled biglycan incubated with equimolar mixtures of ␤ig-h3 and pepsin-collagen VI was increased 6-fold over ␤ig-h3 alone and 3-fold over collagen VI alone. Similar increases were also observed for decorin. The findings indicate that ␤ig-h3 participates in a ternary complex with collagen VI and SLRPs. Static light scattering techniques were used to show that ␤ig-h3 rapidly forms very high molecular weight complexes with both native and pepsin-collagen VI, either alone or with the SLRPs. Indeed ␤ig-h3 was shown to form a complex with collagen VI and biglycan, which appeared to be much more extensive than that formed by ␤ig-h3 with collagen VI and decorin or those formed between the collagen and ␤ig-h3, biglycan, or decorin alone. Biglycan core protein was shown to inhibit the extent of complexing of ␤ig-h3 with native and pepsin-collagen VI suggesting that the glycosaminoglycan side chains of the proteoglycan were important for the formation of the large ternary complexes. Further studies showed that the direct interaction between ␤ig-h3 and biglycan and between biglycan and collagen VI were also important for the formation of these complexes. The globular domains of collagen VI also appeared to have an influence on the interaction of the three components. Overall the results indicate that ␤ig-h3 can differentially modulate the aggregation of collagen VI with biglycan and decorin. Thus this interplay is likely to be important in tissues such as cornea where such complexes are considered to occur.Transforming growth factor-␤ (TGF-␤) 2 -inducible gene-h3 (␤ig-h3) (also known variously as MP78/70 (1, 2), RGD-CAP (3), and keratoepithelin (4)), is an extracellular matrix protein expressed in a wide variety of tissues including developing nuchal ligament, aorta, lung, kidney, and cartilage; and mature cornea, skin, bladder, and bone (5-11). The name ␤ig-h3 stems from its identification and cloning as a major TGF-␤-responsive gene in A549 lung adenocarcinoma cells (12, 13). ␤ig-h3 protein is 76 -78 kDa in size and contains four repeat domains, with homology to the insect protein fasciclin, and 11 cysteine residues most of which ar...

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Novel Fold Revealed by the Structure of a FAS1 Domain Pair from the Insect Cell Adhesion Molecule Fasciclin I

Cited by 100 publications

References 26 publications

A speculation on the tandem fasciclin 1 repeat of FLA4 proteins in angiosperms

A speculation on the tandem fasciclin 1 repeat of FLA4 proteins in angiosperms

Structure of phycobilisome from the red alga Griffithsia pacifica

βig-h3 Interacts Directly with Biglycan and Decorin, Promotes Collagen VI Aggregation, and Participates in Ternary Complexing with These Macromolecules

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