Unraveling CAF-1 family in Plasmodium falciparum: comparative genome-wide identification and phylogenetic analysis among eukaryotes, expression profiling and protein–protein interaction studies

Kaushik, Manjeri; Nehra, Ashima; Gill, Sarvajeet Singh; Gill, Ritu

doi:10.1007/s13205-020-2096-7

Cited by 3 publications

(3 citation statements)

References 55 publications

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“…As CAF-1 family members, they show structural and functional consistency. PfRBBP4, central in malaria biology with 108 PPIs, emerges as a potential antimalarial drug target ( 177 ). Thus, the function of PfRBBP4/7 in P. falciparum illustrates their potential as targets to develop novel antimalarial interventions.…”

Section: Expression and Function Of Rbbp4/7 In Diseasesmentioning

confidence: 99%

Interpreting the molecular mechanisms of RBBP4/7 and their roles in human diseases (Review)

Zhan,

Yin,

et al. 2024

Int J Mol Med

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Histone chaperones serve a pivotal role in maintaining human physiological processes. They interact with histones in a stable manner, ensuring the accurate and efficient execution of DNA replication, repair and transcription. Retinoblastoma binding protein (RBBP)4 and RBBP7 represent a crucial pair of histone chaperones, which not only govern the molecular behavior of histones H3 and H4, but also participate in the functions of several protein complexes, such as polycomb repressive complex 2 and nucleosome remodeling and deacetylase, thereby regulating the cell cycle, histone modifications, DNA damage and cell fate. A strong association has been indicated between RBBP4/7 and some major human diseases, such as cancer, age-related memory loss and infectious diseases. The present review assesses the molecular mechanisms of RBBP4/7 in regulating cellular biological processes, and focuses on the variations in RBBP4/7 expression and their potential mechanisms in various human diseases, thus providing new insights for their diagnosis and treatment.

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Section: Expression and Function Of Rbbp4/7 In Diseasesmentioning

confidence: 99%

Interpreting the molecular mechanisms of RBBP4/7 and their roles in human diseases (Review)

Zhan,

Yin,

et al. 2024

Int J Mol Med

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“…Up to eight different modifications, including phosphorylation, acetylation, and glycosylation, were observed in BiP (also known as HSP70 or Grp78), enolase, and other proteins [ 263 ]. Acetylation and redox modifications, glutathionylation and nitrosylation, were found in chromatin assembly factor 1 (CAF-1) subunit C [ 286 ], implicated in depositing histones on replicated DNA [ 263 ]. Chromatin assembly-binding and DNA-binding proteins were found to undergo methylation at arginine residues, acetylation, ubiquitination, and nitrosylation.…”

Section: Protein Ptms In Plasmodium Parasite Growt...mentioning

confidence: 99%

Post-Translational Modifications of Proteins of Malaria Parasites during the Life Cycle

Schwarzer,

Skorokhod

2024

IJMS

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Post-translational modifications (PTMs) are essential for regulating protein functions, influencing various fundamental processes in eukaryotes. These include, but are not limited to, cell signaling, protein trafficking, the epigenetic control of gene expression, and control of the cell cycle, as well as cell proliferation, differentiation, and interactions between cells. In this review, we discuss protein PTMs that play a key role in the malaria parasite biology and its pathogenesis. Phosphorylation, acetylation, methylation, lipidation and lipoxidation, glycosylation, ubiquitination and sumoylation, nitrosylation and glutathionylation, all of which occur in malarial parasites, are reviewed. We provide information regarding the biological significance of these modifications along all phases of the complex life cycle of Plasmodium spp. Importantly, not only the parasite, but also the host and vector protein PTMs are often crucial for parasite growth and development. In addition to metabolic regulations, protein PTMs can result in epitopes that are able to elicit both innate and adaptive immune responses of the host or vector. We discuss some existing and prospective results from antimalarial drug discovery trials that target various PTM-related processes in the parasite or host.

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“…It represents an evolutionarily conserved histone chaperone complex essential for various fundamental processes in eukaryotes, including chromatin repair following DNA synthesis, cell cycle progression, as well as the establishment and maintenance of heterochromatin [12][13][14]. In most eukaryotes, CAF-1 is a heterotrimeric complex comprising the large subunit p150/CHAF1A, the medium subunit p60/CHAF1B, and the small subunit p48/CHAF1C [15][16][17]. The CHAF1B contains seven WD40 repeats and a B-domain-like motif that binds to Asf1 [18,19].…”

Section: Introductionmentioning

confidence: 99%

Independent and Complementary Functions of Caf1b and Hir1 for Chromatin Assembly in Tetrahymena thermophila

Hao,

Ren,

Lian

et al. 2023

Cells

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Histones and DNA associate to form the nucleosomes of eukaryotic chromatin. Chromatin assembly factor 1 (CAF-1) complex and histone regulatory protein A (HIRA) complex mediate replication-couple (RC) and replication-independent (RI) nucleosome assembly, respectively. CHAF1B and HIRA share a similar domain but play different roles in nucleosome assembly by binding to the different interactors. At present, there is limited understanding for the similarities and differences in their respective functions. Tetrahymena thermophila contains transcriptionally active polyploid macronuclei (MAC) and transcriptionally silent diploid micronuclei (MIC). Here, the distribution patterns of Caf1b and Hir1 exhibited both similarities and distinctions. Both proteins localized to the MAC and MIC during growth, and to the MIC during conjugation. However, Hir1 exhibited additional signaling on parental MAC and new MAC during sexual reproduction and displayed a punctate signal on developing anlagen. Caf1b and Hir1 only co-localized in the MIC with Pcna1 during conjugation. Knockdown of CAF1B impeded cellular growth and arrested sexual reproductive development. Loss of HIR1 led to MIC chromosome defects and aborted sexual development. Co-interference of CAF1B and HIR1 led to a more severe phenotype. Moreover, CAF1B knockdown led to the up-regulation of HIR1 expression, while knockdown of HIR1 also led to an increase in CAF1B expression. Furthermore, Caf1b and Hir1 interacted with different interactors. These results showed that CAF-1 and Hir1 have independent and complementary functions for chromatin assembly in T. thermophila.

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Unraveling CAF-1 family in Plasmodium falciparum: comparative genome-wide identification and phylogenetic analysis among eukaryotes, expression profiling and protein–protein interaction studies

Cited by 3 publications

References 55 publications

Interpreting the molecular mechanisms of RBBP4/7 and their roles in human diseases (Review)

Interpreting the molecular mechanisms of RBBP4/7 and their roles in human diseases (Review)

Post-Translational Modifications of Proteins of Malaria Parasites during the Life Cycle

Independent and Complementary Functions of Caf1b and Hir1 for Chromatin Assembly in Tetrahymena thermophila

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