Extranuclear Histones in Teleost Gills: An Evolutionary Study

Stekhoven, F.M.A.H. Schuurmans; Bonga, S.E. Wendelaar; Flik, G.

doi:10.1007/s10695-005-7442-5

Cited by 11 publications

(3 citation statements)

References 51 publications

(45 reference statements)

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“…Histones H2A and H2B have been found in microsomes from gill epithelium of five species of primitive to advanced teleost fish, indicating that these proteins might be secreted to the extracellular environment [ 45 ]. In addition, histone H2A has been shown to be synthesized in excess, in amounts required for DNA packaging, and accumulates in cytoplasmic granules in gastric gland cells.…”

Section: Discussionmentioning

confidence: 99%

Revealing Natural Intracellular Peptides in Gills of Seahorse Hippocampus reidi

et al. 2023

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The seahorse is a marine teleost fish member of the Syngnathidae family that displays a complex variety of morphological and reproductive behavior innovations and has been recognized for its medicinal importance. In the Brazilian ichthyofauna, the seahorse Hippocampus reidi is among the three fish species most used by the population in traditional medicine. In this study, a protocol was performed based on fast heat inactivation of proteases plus liquid chromatography coupled to mass spectrometry to identify native peptides in gills of seahorse H. reidi. The MS/MS spectra obtained from gills allowed the identification of 1080 peptides, of which 1013 peptides were present in all samples and 67 peptide sequences were identified in an additional LC-MS/MS run from an alkylated and reduced pool of samples. The majority of peptides were fragments of the internal region of the amino acid sequence of the precursor proteins (67%), and N- and C-terminal represented 18% and 15%, respectively. Many peptide sequences presented ribosomal proteins, histones and hemoglobin as precursor proteins. In addition, peptide fragments from moronecidin-like protein, described with antimicrobial activity, were found in all gill samples of H. reidi. The identified sequences may reveal new bioactive peptides.

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Section: Discussionmentioning

confidence: 99%

Revealing Natural Intracellular Peptides in Gills of Seahorse Hippocampus reidi

et al. 2023

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“…Furthermore other explanation may involve ribonucleoproteins known to interact with fibrillarin that can form U bodies structures found in the cytoplasm ( Liu and Gall, 2007 ) although it is unclear why methylation of H2A would be required for this outside the nucleus. Although it is known those histones H2A/H2B have antimicrobial action in particular cells that are closer to the surface as publish ( Stekhoven et al, 2004 ). The absence of this signal in vascular inflorescence cells can be due to a reduction in the number of mitochondria for this cell type or lack of U bodies.…”

Section: Discussionmentioning

confidence: 99%

Fibrillarin methylates H2A in RNA polymerase I trans-active promoters in Brassica oleracea

et al. 2015

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Fibrillarin is a well conserved methyltransferase involved in several if not all of the more than 100 methylations sites in rRNA which are essential for proper ribosome function. It is mainly localized in the nucleoli and Cajal bodies inside the cell nucleus where it exerts most of its functions. In plants, fibrillarin binds directly the guide RNA together with Nop56, Nop58, and 15.5ka proteins to form a snoRNP complex that selects the sites to be methylated in pre-processing of ribosomal RNA. Recently, the yeast counterpart NOP1 was found to methylate histone H2A in the nucleolar regions. Here we show that plant fibrillarin can also methylate histone H2A. In Brassica floral meristem cells the methylated histone H2A is mainly localized in the nucleolus but unlike yeast or human cells it also localize in the periphery of the nucleus. In specialized transport cells the pattern is altered and it exhibits a more diffuse staining in the nucleus for methylated histone H2A as well as for fibrillarin. Here we also show that plant fibrillarin is capable of interacting with H2A and carry out its methylation in the rDNA promoter.

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“…Although Amyloodinium does not affect freshwater fish such as channel catfish, proteins homologous to HbβP‐1 are present in microsomes of gill cells from a number of teleosts including Mozambique tilapia, Oreochromis mossambicus (Peters), rainbow trout, common carp, Cyprinus carpio L., European eel, Anguilla anguilla (L.), and elephant fish, Gnathonemus petersii (Günther) (Stekhoven, Bonga & Flik 2004). The presence of Hb‐β in microsomes from gill epithelium of primitive to advanced teleosts, some of which (trout and eel) spend part of their lives in sea water, suggests that Hb‐β‐derived AMPs like those isolated from the channel catfish may be expected even in marine fish.…”

Section: Discussionmentioning

confidence: 99%

Antiparasitic activity of the antimicrobial peptide HbβP‐1, a member of the β‐haemoglobin peptide family

Ullal

Noga

2010

Journal of Fish Diseases

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A family of antimicrobial peptides (AMPs) derived from the beta-subunit of haemoglobin was recently isolated from channel catfish, Ictalurus punctatus, infected with Ichthyophthirius multifiliis (ich), an important freshwater fish parasite that causes ichthyophthiriosis. We previously discovered that one of these AMPs, HbbetaP-1, had strong cidal activity against ich as well as another ectoparasite, Tetrahymena pyriformis. HbbetaP-1 toxicity was specific, primarily affecting the trophozoite (trophont) stage of ich. Here, we show that HbbetaP-1 acts more rapidly to kill smaller (presumably less mature) trophonts of ich, taking almost twice as long to kill larger trophonts (P < 0.0001). It acts more rapidly than an unrelated AMP, piscidin 1, which is haemolytic and also lethal to ich trophonts. HbbetaP-1 is potently and selectively lethal to the trophont stage of the dinoflagellate ectoparasite, Amyloodinium ocellatum, one of the most important pathogens of warmwater marine fish. HbbetaP-1 has no effect on the fish gill cell line feeder layer (G1B cells) used to propagate Amyloodinium, further suggesting a highly selective action. These findings suggest that HbbetaP-1 or related AMPs might function in protecting marine as well as freshwater fish and that HbbetaP-1 has highly selective activity against specific life stages of important fish ectoparasites.

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Extranuclear Histones in Teleost Gills: An Evolutionary Study

Cited by 11 publications

References 51 publications

Revealing Natural Intracellular Peptides in Gills of Seahorse Hippocampus reidi

Revealing Natural Intracellular Peptides in Gills of Seahorse Hippocampus reidi

Fibrillarin methylates H2A in RNA polymerase I trans-active promoters in Brassica oleracea

Antiparasitic activity of the antimicrobial peptide HbβP‐1, a member of the β‐haemoglobin peptide family

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