Evolution of distinct EGF domains with specific functions

Wouters, Merridee A.; Rigoutsos, Isidore; Chu, Carmen K.; Feng, Lina L.; Sparrow, Duncan B.; Dunwoodie, Sally L.

doi:10.1110/ps.041207005

Cited by 151 publications

(148 citation statements)

References 62 publications

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“…A modeling study had suggested that residues 293-346 of eSRK6 encode an EGF-like domain [17] that is principally defined by six cysteines, which are known to form disulphide bonds in a 1-3, 2-4, and 5-6 pattern [25]. Indeed, this region of eSRK9 forms a structure that can be largely aligned with that of EGF [26] ( Figure 2C).…”

Section: The S-domain Architecture Of Esrk9mentioning

confidence: 99%

Structural basis for specific self-incompatibility response in Brassica

Han

et al. 2016

Cell Res

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Self-incompatibility (SI) is a widespread mechanism in flowering plants which prevents self-fertilization and inbreeding. In Brassica, recognition of the highly polymorphic S-locus cysteine-rich protein (SCR; or S-locus protein 11) by the similarly polymorphic S-locus receptor kinase (SRK) dictates the SI specificity. Here, we report the crystal structure of the extracellular domain of SRK9 (eSRK9) in complex with SCR9 from Brassica rapa. SCR9 binding induces eSRK9 homodimerization, forming a 2:2 eSRK:SCR heterotetramer with a shape like the letter "A". Specific recognition of SCR9 is mediated through three hyper-variable (hv) regions of eSRK9. Each SCR9 simultaneously interacts with hvI and one-half of hvII from one eSRK9 monomer and the other half of hvII from the second eSRK9 monomer, playing a major role in mediating SRK9 homodimerization without involving interaction between the two SCR9 molecules. Single mutations of residues critical for the eSRK9-SCR9 interaction disrupt their binding in vitro. Our study rationalizes a body of data on specific recognition of SCR by SRK and provides a structural template for understanding the co-evolution between SRK and SCR.

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Section: The S-domain Architecture Of Esrk9mentioning

confidence: 99%

Structural basis for specific self-incompatibility response in Brassica

Han

et al. 2016

Cell Res

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“…Multiple modules, EF-hands, C2 domains, and EGF domains, have purposes such as sensing and sequestration of Ca 2ϩ (5,7,58,59), and Ca 2ϩ binding takes place at a specific motif forming continuous or discontinuous Ca 2ϩ -binding sites (60,61). The EF-hand motif, an example of a continuous site, is the predominant class in CaBP.…”

Section: ؉ -Binding Motifsmentioning

confidence: 99%

Ca2+-binding Motif of βγ-Crystallins

Srivastava¹,

Mishra

Krishnan³

et al. 2014

Journal of Biological Chemistry

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␤␥-Crystallin-type double clamp (N/D)(N/D)XX(S/T)S motif is an established but sparsely investigated motif for Ca2؉ binding. A ␤␥-crystallin domain is formed of two Greek key motifs, accommodating two Ca 2؉ -binding sites. ␤␥-Crystallins make a separate class of Ca 2؉ -binding proteins (CaBP), apparently a major group of CaBP in bacteria. Paralleling the diversity in ␤␥-crystallin domains, these motifs also show great diversity, both in structure and in function. Although the expression of some of them has been associated with stress, virulence, and adhesion, the functional implications of Ca 2؉ binding to ␤␥-crystallins in mediating biological processes are yet to be elucidated.

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“…Threading tools return with low score alignments to EGF modules (PDB ID code 1KLO), but there is no strong consensus from the different contributing servers on the structure of this fragment. It should be noted, however, that EGF modules are often difficult to identify (21) because highly diverged amino acid sequences can adopt an EGF-type protein fold (22) (SI Fig. 9B).…”

Section: Identification Of Structural Modules Within Esrk By Homologymentioning

confidence: 99%

Structural modules for receptor dimerization in the S -locus receptor kinase extracellular domain

Naithani¹,

Chookajorn²,

Ripoll

et al. 2007

Proc. Natl. Acad. Sci. U.S.A.

109

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The highly polymorphic S-locus receptor kinase (SRK) is the stigma determinant of specificity in the self-incompatibility response of the Brassicaceae. SRK spans the plasma membrane of stigma epidermal cells, and it is activated in an allele-specific manner on binding of its extracellular region (eSRK) to its cognate pollen coat-localized S-locus cysteine-rich (SCR) ligand. SRK, like several other receptor kinases, forms dimers in the absence of ligand. To identify domains in SRK that mediate ligand-independent dimerization, we assayed eSRK for self-interaction in yeast. We show that SRK dimerization is mediated by two regions in eSRK, primarily by a C-terminal region inferred by homology modeling/fold recognition techniques to assume a PAN APPLE-like structure, and secondarily by a region containing a signature sequence of the S-domain gene family, which might assume an EGF-like structure. We also show that eSRK exhibits a marked preference for homodimerization over heterodimerization with other eSRK variants and that this preference is mediated by a small, highly variable region within the PAN APPLE domain. Thus, the extensive polymorphism exhibited by the eSRK not only determines differential affinity toward the SCR ligand, as has been assumed thus far, but also underlies a previously unrecognized allelic specificity in SRK dimerization. We propose that preference for SRK homodimerization explains the codominance exhibited by a majority of SRKs in the typically heterozygous stigmas of self-incompatible plants, whereas an increased propensity for heterodimerization combined with reduced affinity of heterodimers for cognate SCRs might underlie the dominant-recessive or mutual weakening relationships exhibited by some SRK allelic pairs.self-incompatibility ͉ ligand-independent receptor dimerization ͉ yeast two-hybrid T he S-locus receptor kinase (SRK) is a single-pass integral plasma membrane protein of the stigma epidermis that functions in the recognition and rejection of self-related pollen in self-incompatible members of the Brassicaceae (reviewed in refs. 1 and 2). The SRK receptor and its pollen-coat localized ligand, the S-locus cysteine-rich protein (SCR) (1), also designated SP-11 (2), are encoded by tightly linked and highly polymorphic genes within the S-locus haplotype. Specificity in the self-incompatibility response derives from allele-specific SRK-SCR interaction (3, 4). On self-pollination, the binding of SCR to the extracellular domain of its cognate SRK activates the receptor and triggers an intracellular signaling cascade that leads to arrest of ''self'' pollen tubes. In contrast, pollen tube growth in cross-pollinations proceeds unimpeded because ''nonself'' SCR cannot bind SRK. In view of this high degree of specificity in the affinity of SRK for its SCR ligand, the extensive polymorphisms exhibited by the SRK extracellular region (eSRK) have heretofore been considered in the context of specificity in the SRK-SCR interaction.The eSRK does more than interact with SCR, however. SRK forms oligo...

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Evolution of distinct EGF domains with specific functions

Cited by 151 publications

References 62 publications

Structural basis for specific self-incompatibility response in Brassica

Structural basis for specific self-incompatibility response in Brassica

Ca2+-binding Motif of βγ-Crystallins

Structural modules for receptor dimerization in the S -locus receptor kinase extracellular domain

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