Cyanobacteria contain a family of genes encoding one-helix high-light-inducible proteins (Hlips) that are homologous to light harvesting chlorophyll a/b-binding proteins of plants and algae. Based on various experimental approaches used for their study, a spectrum of functions that includes regulation of chlorophyll biosynthesis, transient chlorophyll binding, quenching of singlet oxygen and non-photochemical quenching of absorbed energy is ascribed to Hlips. However, these functions had not been supported by conclusive experimental evidence until recently when it became clear that Hlips are able to quench absorbed light energy and assist during terminal step(s) of the chlorophyll biosynthesis and early stages of Photosystem II assembly. In this review we summarize and discuss the present knowledge about Hlips and provide a model of how individual members of the Hlip family operate during the biogenesis of chlorophyll-proteins, namely Photosystem II. This article is part of a Special Issue entitled Organization and dynamics of bioenergetic systems in bacteria, edited by Conrad Mullineaux.

Institute of Microbiology Laboratory of Photosynthesis Centre Algatech 37901 Třeboň Czech Republic; Faculty of Science University of South Bohemia 370 05 České Budějovice Czech Republic

Citace poskytuje Crossref.org

The Role of FtsH Complexes in the Response to Abiotic Stress in Cyanobacteria

FtsH4 protease controls biogenesis of the PSII complex by dual regulation of high light-inducible proteins

Assembly of D1/D2 complexes of photosystem II: Binding of pigments and a network of auxiliary proteins

Psb34 protein modulates binding of high-light-inducible proteins to CP47-containing photosystem II assembly intermediates in the cyanobacterium Synechocystis sp. PCC 6803

Plant LHC-like proteins show robust folding and static non-photochemical quenching

The Influence of Metabolic Inhibitors, Antibiotics, and Microgravity on Intact Cell MALDI-TOF Mass Spectra of the Cyanobacterium Synechococcus Sp. UPOC S4

Sequential deletions of photosystem II assembly factors Ycf48, Ycf39 and Pam68 result in progressive loss of autotrophy in the cyanobacterium Synechocystis PCC 6803

The antenna-like domain of the cyanobacterial ferrochelatase can bind chlorophyll and carotenoids in an energy-dissipative configuration

Plant and algal chlorophyll synthases function in Synechocystis and interact with the YidC/Alb3 membrane insertase

Binding of pigments to the cyanobacterial high-light-inducible protein HliC

Molecular Origin of Photoprotection in Cyanobacteria Probed by Watermarked Femtosecond Stimulated Raman Spectroscopy

Twisting a β-Carotene, an Adaptive Trick from Nature for Dissipating Energy during Photoprotection

A method to decompose spectral changes in Synechocystis PCC 6803 during light-induced state transitions