2022
DOI: 10.3390/molecules27020378
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Structural Identification of Metalloproteomes in Marine Diatoms, an Efficient Algae Model in Toxic Metals Bioremediation

Abstract: The biosorption of pollutants using microbial organisms has received growing interest in the last decades. Diatoms, the most dominant group of phytoplankton in oceans, are (i) pollution tolerant species, (ii) excellent biological indicators of water quality, and (iii) efficient models in assimilation and detoxification of toxic metal ions. Published research articles connecting proteomics with the capacity of diatoms for toxic metal removal are very limited. In this work, we employed a structural based systema… Show more

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Cited by 10 publications
(7 citation statements)
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“…In addition, peeling Cu compound particles can become marine pollutants. There is no doubt that they will have different effects on marine organisms [ 33 , 34 , 35 ]. This study did not examine seafloor sediments, so the behavior of type C, which contains copper compounds, on the seafloor remains unclear.…”
Section: Resultsmentioning
confidence: 99%
“…In addition, peeling Cu compound particles can become marine pollutants. There is no doubt that they will have different effects on marine organisms [ 33 , 34 , 35 ]. This study did not examine seafloor sediments, so the behavior of type C, which contains copper compounds, on the seafloor remains unclear.…”
Section: Resultsmentioning
confidence: 99%
“…Copper (Cu) adsorption and uptake were reported in the diatom under enhanced nitrogen and phosphorous intake Phaeodactylum tricornutum (Zhou et al 2022). Metalloproteome engulfs about 13% of total diatom proteome in heavy metal accumulation and detoxi cation including Hg, Cd, Pb, Cr, As, and Ba (Chasapis et al 2022).…”
Section: Discussionmentioning
confidence: 99%
“…The structures of E3 ligases RNF41, TRIM59, and MIB1 have yet to be determined experimentally. Zinc binding amino acid motifs of RNF41, TRIM59 and MIB1 were characterized using the strategy previously applied to identify putative metal-binding sites in various proteomes [19] , [20] , [21] , [22] , [23] . The list of known zinc binding domains (such as: SIAH-type Zn(II) finger, B-box type Zn (II) finger, ZZ-type Zn(II) finger and zinc domains of metalloproteases [24] , has been extracted from the Pfam library ( http://pfam.xfam.org/ ) [25] , and their 3D structures were retrieved from the Protein Data Bank (PDB; http://www.rcsb.org/pdb/ ) [26] and MetalPDB databases ( https://metalpdb.cerm.unifi.it/ ) [27] .…”
Section: Methodsmentioning
confidence: 99%