Yehishalom, N. | Search bioRxiv

bioRxiv2023

The protein phosphorylation landscape in photosystem I of the desert algae Chlorella sp.

O_LIThe phosphorylation of photosystem II (PSII) and its antenna (LHCII) proteins has been extensively studied and its involvement in state transitions and PSII repair is well known. Yet, very little is known about the extent and functions of phosphorylation of photosystem I (PSI) and its antenna (LHCI) proteins. C_LIO_LIHere, two proteomics methods were applied to generate a detailed map of the phosphorylation sites of the PSI-LHCI proteins in Chlorella ohadii cells that were grown under low- or extreme high-light intensities (LL and HL). Furthermore, we analyzed the content of oxidized tryptophans in these cell types to estimate light-induced oxidative damage to PSI-LHCI. C_LIO_LIOur work revealed the phosphorylation of 11 out of 22 PSI-LHCI subunits. The analyses detected extensive phosphorylation of the LHCI subunits lhca6 and lhca7. Other PSI-LHCI subunits were phosphorylated to a lesser extent. Additionally, we show the accumulation of oxidatively damaged tryptophans in the psaD subunit of PSI of HL-grown C. ohadii. C_LIO_LIThe significant phosphorylation of lhca6 and lhca7 suggests a physiological role during photosynthesis, possibly by altering light-harvesting characteristics and binding of other LHCI subunits. Moreover, we show that psaD is susceptible to photodamage while LHCI is protected from ROS under HL. C_LI

plant biology↗

bioRxiv2022

Defining amino acid pairs as structural units suggests mutation sensitivity toadjacent residues

Proteins fold from chains of amino acids, forming secondary structures, -helices and {beta}-strands, that, at least for globular proteins, subsequently fold into a three-dimensional structure. A large-scale analysis of high-resolution protein structures suggests that amino acid pairs constitute another layer of ordered structure, more local than these conventionally defined secondary structures. We develop a cross-peptide-bond Ramachandran plot that captures the conformational preferences of the amino acid pairs and show that the effect of a particular mutation on the stability of a protein depends in a predictable manner on the adjacent amino acid context. One-Sentence SummaryLarge-scale protein backbone analysis reveals amino acid pair conformational preferences and predicts how sequence context affects mutant stability.

molecular biology↗