Chlorophyll a/b binding-specificity in water-soluble chlorophyll protein

Palm, Daniel M.; Agostini, Alessandro; Averesch, V.; Girr, Philipp; Werwie, Mara; Takahashi, Shingo; Satoh, Hiroyuki; Jaenicke, Elmar; Paulsen, Harald

doi:10.1038/s41477-018-0273-z

Cited by 47 publications

(70 citation statements)

References 51 publications

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“…Multiple sequence alignment of the extended set of 18 nonredundant natural WSCP sequences and their five ASR‐generated archetypes were mapped onto the representative type‐IIa, and type‐IIb molecular structures of CaWSCP , and LvWSCP . Both sequence and structural alignments pointed to specific sites of Chl‐protein and protein–protein interactions that may impact Chl‐binding specificity, bound Chl spectra, and assembly of the homotetrameric complex.…”

Section: Resultsmentioning

confidence: 99%

“…In type‐IIa, the loop is extended by two residues as compared to type‐IIb, with proline, and glutamate or aspartate (P88, and D/E92 in CaWSCP) inserted at the first, and fourth positions, respectively following the conserved tryptophan. Mutations in this region were shown to affect the binding preferences for Chl a vs Chl b in type‐IIa and type‐IIb WSCPs .…”

Section: Discussionmentioning

confidence: 99%

“…In type-IIa, the loop is extended by two residues as compared to type-IIb, with proline, and glutamate or aspartate (P88, and D/E92 in CaWSCP) inserted at the first, and fourth positions, respectively following the conserved tryptophan. Mutations in this region were shown to affect the binding preferences for Chl a vs Chl b in type-IIa and type-IIb WSCPs [31]. Extension of the Chl-binding WSCPs database, particularly by the discovery of new members of the type-IIb subclass, sheds light on the tuning mechanisms of Chl spectra by the protein environment.…”

Section: Determinants Of Chlorophyll Binding Complex Assembly and Smentioning

confidence: 99%

“…, and Palm et al . elucidated some molecular determinants of Chl absorption band shifts, and Chl a/b ‐binding selectivity, respectively.…”

Section: Introductionmentioning

confidence: 99%

“…Recently developed methods for assembling recombinant WSCP apo-proteins with natural and synthetic Chl derivatives [28][29][30], now render the complex an ideal system for rigorous spectroscopic and biochemical studies. Indeed, by combining these methods with X-ray crystallography and site-directed mutagenesis, Bednarczyk et al [26], and Palm et al [31] elucidated some molecular determinants of Chl absorption band shifts, and Chl a/b-binding selectivity, respectively.…”

Section: Introductionmentioning

confidence: 99%

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New homologues of Brassicaceae water‐soluble chlorophyll proteins shed light on chlorophyll binding, spectral tuning, and molecular evolution

et al. 2019

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Type‐II water‐soluble chlorophyll (Chl) proteins (WSCPs) of Brassicaceae are promising models for understanding how protein sequence and structure affect Chl binding and spectral tuning in photosynthetic Chl–protein complexes. However, to date, their use has been limited by the small number of known WSCPs, which also limited understanding their physiological roles. To overcome these limitations, we performed a phylogenetic analysis to compile a more comprehensive and complete set of natural type‐II WSCP homologues. The identified homologues were heterologously expressed in Escherichia coli, purified, tested for assembly with chlorophylls, and spectroscopically characterized. The analyses led to the discovery of previously unrecognized type‐IIa and IIb subclass WSCPs, as well as of a new subclass that did not bind chlorophylls. Further analysis by ancestral sequence reconstruction yielded sequences of putative ancestors of the three subclasses, which were subsequently recombinantly expressed in E. coli, purified and characterized. Combining the phylogenetic and spectroscopic data with molecular structural information revealed distinct Chl‐binding motifs, and identified residues critically impacting spectral tuning. The distinct Chl‐binding properties of the WSCP archetypes suggest that the non‐Chl‐binding subclass evolved from a Chl‐binding ancestor that most likely lost its Chl‐binding capacity upon localization in the plant tissues with low Chl content. This dual evolutionary trajectory is consistent with WSCPs association with the Kunitz‐type protease inhibitors superfamily, and indications of their inhibitory activity in response to various forms of stress in plants. These findings suggest new directions for exploring the physiological roles of WSCPs and the correlation, if any, between Chl‐binding and protease inhibition functionality.

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Section: Resultsmentioning

confidence: 99%

Section: Discussionmentioning

confidence: 99%

Section: Determinants Of Chlorophyll Binding Complex Assembly and Smentioning

confidence: 99%

“…, and Palm et al . elucidated some molecular determinants of Chl absorption band shifts, and Chl a/b ‐binding selectivity, respectively.…”

Section: Introductionmentioning

confidence: 99%