Synthesis and turnover of the light-harvesting chlorophylla/b-protein inLemna gibba grown with intermittent red light: possible translational control

Planta ◽  
1982 ◽  
Vol 154 (5) ◽  
pp. 465-472 ◽  
Author(s):  
J. P. Slovin ◽  
E. M. Tobin

2021 ◽  
Vol 258 ◽  
pp. 123932
Author(s):  
Lekha Peedikakkandy ◽  
Ondřej Pavelka ◽  
Martina Alsterová ◽  
Anna Fučíková ◽  
Jakub Dostál ◽  
...  


1998 ◽  
Vol 53 (11-12) ◽  
pp. 1017-1026 ◽  
Author(s):  
A. Kiinne ◽  
E. Pistorius ◽  
K. Kloppstech ◽  
E. de Groot

Abstract Two proteins with apparent molecular masses of 17 and 24 kD that are synthesized in a circadian manner in the phytoflagellate Euglena gracilis, were recognized as proteins belong­ing to the family of light-harvesting-chlorophyll-proteins (LHCPs) of class I (17 kD) and of class II (24 kD). Identification was achieved by N-terminal sequencing of the proteins isolated from two-dimensional polyacrylamide gels and by detection with an anti-LHCP II se­rum. While it was found that the total amount of LHCPs remains almost constant, when Euglena is grown under diurnal conditions (12 h light and 12 h dark), we could show that the amount of newly synthesized 17 and 24 kD proteins varies about 20-fold with a maximum of synthesis in the light phase. In contrast, the analysis of the mRNA levels at different times revealed only minor differences in the stationary concentration of the LHCP specific mRNA, indicating that the control of LHCP synthesis is at the translational level. Principally, the same finding was obtained using inhibitors of transcription. Thus, it is concluded that the expression of LHCPs in Euglena gracilis in contrast to that of higher plants is primarily regulated at the translational level.



1975 ◽  
Vol 2 (2) ◽  
pp. 129
Author(s):  
M.E Gordon ◽  
D.S Letham

The cytokinin 6-benzylaminopurine (BAP) markedly stimulated the lateral expansion of excised immature radish cotyledons after a lag period of about 10 h. This growth occurred principally by cell enlargement, especially in the light which enhanced the response. However, a marked response 'to cytokinin occurred in the complete absence of red light during germination, cotyledon excision and incubation. Contact with BAP for 5 h significantly stimulated growth, but a maximum response required more than 24 h of contact; potassium chloride also promoted cotyledon expansion and acted synergistically with cytokinin. The response to cytokinin did not appear to be mediated by ethylene, gibberellins, polyamines or cyclic nucleotides. Growth induction did not alter the respiration rate and appeared to be inde- pendent of chloroplast function. Inhibitors of DNA and RNA synthesis and of protein synthesis on cytoplasmic ribosomes almost completely abolished BAP-induced growth, control growth being less markedly affected. There were, however, no significant BAP-induced increases in total DNA or RNA levels or specific activity before the initiation of growth stimulation. Similarly, BAP had no effect on any individual RNA species until after the lag period, when there was a small enhancement of uridine incorporation into RNA species with similar electrophoretic mobility to rRNA. Although total protein levels were not affected by BAP, the cytokinin enhanced amino acid incorporation into protein within the lag period, an effect which persisted when transcription was strongly inhibited by actinomycin D. Phosphorylation of total protein was stimulated by BAP only well after the onset of cytokinin-induced growth. Protein methylation, however, was stimulated by BAP during the lag period, and the effect was at least as early as the BAP-enhanced incorporation of methionine into protein. The possible role of translational control in the mechanism of cytokinin action is discussed.



Chloroplast development involves the nucleus, the cytoplasm and the chloroplast of plant cells. This may be illustrated by reference to the two most abundant proteins of the chloroplast: (i) the soluble CO 2 -fixing enzyme ribulose 1,5-bisphosphate carboxylase—oxygenase, whose large subunit (LSU) is encoded in chloroplast DNA and synthesized on chloroplast ribosomes and whose small subunit (SSU) is encoded in nuclear DNA, synthesized on cytoplasmic ribosomes in precursor form and transported into chloroplasts, and (ii) the thylakoid-bound light-harvesting chlorophyll a/b complex, whose pigment components are synthesized in the chloroplast and whose apoproteins resemble the SSU in site of coding and site of synthesis. We have examined the extent to which biosynthetic events in the nucleocytoplasmic compartments are coordinated with those inside the chloroplast during the de-etiolation of pea seedlings. We have examined the levels of LSU, SSU and the light-harvesting chlorophyll a/b protein (LHCP) by using a highly specific radioimmune assay. The steady-state levels of the corresponding mRNAs have been determined using specific cloned DNA probes. With the SSU, the mRNA and protein levels are near the limit of detection in dark-grown plants but increase markedly under continuous white light, with a lag of about 24 h. The protein appears to be under simple phytochrome control at the level of the steady-state concentration of its mRNA. The LSU also appears to be regulated through the steady-state concentration of its mRNA but in this case the mRNA is not under simple phytochrome control. The LHCP mRNA is readily detectable in dark-grown plants and accumulates further under illumination in a phytochrome-mediated manner. However, the LHCP itself (like chlorophyll) is not detectable in dark-grown plants and accumulates to high levels only under continuous illumination, with a lag of about 6 h. Post-translational control is particularly important in the accumulation of the LHCP: continuous chlorophyll synthesis is required for the stabilization of the protein within the thylakoid membrane, at least during the early stages of chloroplast development.



2009 ◽  
Vol 20 (40) ◽  
pp. 405207 ◽  
Author(s):  
Yun-Yue Lin ◽  
Di-Yan Wang ◽  
Hung-Chi Yen ◽  
Hsuen-Li Chen ◽  
Chia-Chun Chen ◽  
...  


Microbiology ◽  
2008 ◽  
Vol 77 (3) ◽  
pp. 339-347 ◽  
Author(s):  
Z. K. Makhneva ◽  
Yu. E. Erokhin ◽  
A. A. Moskalenko


2015 ◽  
Vol 14 (10) ◽  
pp. 1826-1830 ◽  
Author(s):  
M. Ertl ◽  
E. Wöβ ◽  
G. Knör

Stable light-harvesting sensitizers for the two-electron oxidation of halide ions are reported. Photocatalysis is studied in solution, in aqueous micellar medium and with surface immobilized samples for convenient photocatalyst recycling.



mBio ◽  
2016 ◽  
Vol 7 (1) ◽  
Author(s):  
Lisa B. Wiltbank ◽  
David M. Kehoe

ABSTRACT The genomes of many photosynthetic and nonphotosynthetic bacteria encode numerous phytochrome superfamily photoreceptors whose functions and interactions are largely unknown. Cyanobacterial genomes encode particularly large numbers of phytochrome superfamily members called cyanobacteriochromes. These have diverse light color-sensing abilities, and their functions and interactions are just beginning to be understood. One of the best characterized of these functions is the regulation of photosynthetic light-harvesting antenna composition in the cyanobacterium Fremyella diplosiphon by the cyanobacteriochrome RcaE in response to red and green light, a process known as chromatic acclimation. We have identified a new cyanobacteriochrome named DpxA that maximally senses teal (absorption maximum, 494 nm) and yellow (absorption maximum, 568 nm) light and represses the accumulation of a key light-harvesting protein called phycoerythrin, which is also regulated by RcaE during chromatic acclimation. Like RcaE, DpxA is a two-component system kinase, although these two photoreceptors can influence phycoerythrin expression through different signaling pathways. The peak responsiveness of DpxA to teal and yellow light provides highly refined color discrimination in the green spectral region, which provides important wavelengths for photosynthetic light harvesting in cyanobacteria. These results redefine chromatic acclimation in cyanobacteria and demonstrate that cyanobacteriochromes can coordinately impart sophisticated light color sensing across the visible spectrum to regulate important photosynthetic acclimation processes. IMPORTANCE The large number of cyanobacteriochrome photoreceptors encoded by cyanobacterial genomes suggests that these organisms are capable of extremely complex light color sensing and responsiveness, yet little is known about their functions and interactions. Our work uncovers previously undescribed cooperation between two photoreceptors with very different light color-sensing capabilities that coregulate an important photosynthetic light-harvesting protein in response to teal, green, yellow, and red light. Other cyanobacteriochromes that have been shown to interact functionally sense wavelengths of light that are close to each other, which makes it difficult to clearly identify their physiological roles in the cell. Our finding of two photoreceptors with broad light color-sensing capabilities and clearly defined physiological roles provides new insights into complex light color sensing and its regulation.





Sign in / Sign up

Export Citation Format

Share Document