ZNHIT2

Last update 08 May 2025

Basic Info

Synonyms

C11orf5, FON, Protein FON

+ [3]

Introduction

May act as a bridging factor mediating the interaction between the R2TP/Prefoldin-like (R2TP/PFDL) complex and U5 small nuclear ribonucleoprotein (U5 snRNP) (PubMed:28561026). Required for the interaction of R2TP complex subunit RPAP3 and prefoldin-like subunit URI1 with U5 snRNP proteins EFTUD2 and PRPF8 (PubMed:28561026). May play a role in regulating the composition of the U5 snRNP complex (PubMed:28561026).

100 Clinical Results associated with ZNHIT2

100 Translational Medicine associated with ZNHIT2

0 Patents (Medical) associated with ZNHIT2

Literatures (Medical) associated with ZNHIT2

01 May 2025·Microbiological Research

Fusarium oxysporum NAD+ hydrolase FonNADase1 is essential for pathogenicity and inhibits plant immune responses

Article

Author: Guo, Mengmeng ; Lou, Jiajun ; Wang, Jiajing ; Li, Dayong ; Xiong, Xiaohui ; Gao, Yizhou ; Song, Fengming

Plants use nicotinamide adenine dinucleotide (NAD⁺) as a key signaling molecule to activate immune responses. However, whether pathogens secrete specific NAD⁺ hydrolases (NADases) to affect plant NAD⁺ levels for infection remains unclear. Here, we report the function and possible mechanism of fungal NADases in watermelon Fusarium wilt fungus Fusarium oxysporum f. sp. niveum (Fon) pathogenicity. Fon secretes two NADases, FonNADase1 and FonNADase2, both of which harbor a secretory signal peptide and an NADase-active tuberculosis necrotizing toxin (TNT) domain. FonNADase1 and FonNADase2 are not involved in the growth, development, or stress responses of Fon. Moreover, only FonNADase1 is essential for Fon pathogenicity, and FonNADase1 deletion results in decreased invasive growth and spread within watermelon plants. FonNADase1 and FonNADase2 are functional NADases capable of decreasing plant NAD⁺ levels and FonNADase1 inhibits INF1- and BAX-induced cell death and chitin-triggered immune responses in Nicotiana benthamiana leaves in an NADase activity-dependent manner. Furthermore, FonNADase1 inhibited INF1- and BAX-induced expression of defense genes, such as NbPR1a, NbPR2, NbLOX, NbERF1, NbHIN1, and NbHSR203J, in N. benthamiana leaves and affected the expression of a set of immunity-associated genes in watermelon plants. These findings suggest that FonNADase1 plays a key role in Fon pathogenicity by affecting fungal invasive growth and spread within plants as well as modulating host immune responses, thus highlighting the critical role of fungal NADases in pathogenicity.

01 Feb 2025·International Journal of Biological Macromolecules

Poly(ADP-ribose) polymerase FonPARP1-catalyzed PARylation of protein disulfide isomerase FonPdi1 regulates pathogenicity of Fusarium oxysporum f. sp. niveum on watermelon

Article

Author: Song, Fengming ; Guo, Mengmeng ; Wang, Jiajing ; Yan, Yuqing ; Lou, Jiajun ; Xiong, Xiaohui ; Li, Dayong ; Noman, Muhammad ; Gao, Yizhou

Poly(ADP-ribosyl)ation (PARylation), catalyzed by poly(ADP-ribose) polymerases (PARPs) and hydrolyzed by poly(ADP-ribose) glycohydrolase (PARG), is an important reversible post-translational protein modification in all eukaryotes, including plant pathogenic fungi. Previously, we revealed that FonPARP1, an active PARP, is crucial for the pathogenicity of Fusarium oxysporum f. sp. niveum (Fon), the causative agent of watermelon Fusarium wilt. This study explores the enzymatic activity and substrates of FonPARP1 in regulating Fon pathogenicity. FonPARP1 is localized in nuclei of Fon macroconidia and hyphae. Essential conserved domains and a key glutamic acid residue at position 729 are critical for FonPARP1 enzyme activity and pathogenicity function in Fon. FonPARP1 interacts with protein disulfide isomerase FonPdi1 and PARylates it at 13 glutamic acid residues, affecting the interaction ability, PDI activity, ER homeostasis, and pathogenicity function. FonPARG1, interacting with both FonPARP1 and FonPdi1, hydrolyzes poly(ADP-ribose) chains from auto-PARylated FonPARP1 and FonPARP1-PARylated FonPdi1. These findings underscore the role of FonPARP1-catalyzed PARylation in regulating Fon pathogenicity and its significance in plant pathogenic fungi.

11 Nov 2024·Biology of Reproduction

Overlapping peri-implantation phenotypes of ZNHIT1 and ZNHIT2 despite distinct functions during early mouse development

Article

Author: Yang, Zhongzhou ; Cui, Wei ; Taylor, Louis F ; Tremblay, Kimberly D ; Mager, Jesse ; Miao, Yi-Liang ; He, Xinjian Doris ; Lin, Xinhua ; Miao, Xiaosu ; Alfandari, Dominique ; Liu, Xin ; Shi, Yingchao

AbstractMammalian preimplantation development culminates in the formation of a blastocyst that undergoes extensive gene expression regulation to successfully implant into the maternal endometrium. Zinc-finger HIT domain-containing (ZNHIT) 1 and 2 are members of a highly conserved family, yet they have been identified as subunits of distinct complexes. Here, we report that knockout of either Znhit1 or Znhit2 results in embryonic lethality during peri-implantation stages. Znhit1 and Znhit2 mutant embryos have overlapping phenotypes, including reduced proportion of SOX2-positive inner cell mass cells, a lack of Fgf4 expression, and aberrant expression of NANOG and SOX17. Furthermore, we find that the similar phenotypes are caused by distinct mechanisms. Specifically, embryos lacking ZNHIT1 likely fail to incorporate sufficient H2A.Z at the promoter region of Fgf4 and other genes involved in cell projection organization resulting in impaired invasion of trophoblast cells during implantation. In contrast, Znhit2 mutant embryos display a complete lack of nuclear EFTUD2, a key component of U5 spliceosome, indicating a global splicing deficiency. Our findings unveil the indispensable yet distinct roles of ZNHIT1 and ZNHIT2 in early mammalian embryonic development.

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ZNHIT2

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