Zinc finger proteins (ZFPs) containing only a single zinc finger domain play important roles in the regulation of plant growth and development, as well as in biotic and abiotic stress responses. To date, the evolutionary history and functions of the ZFP gene family have not been identified in cotton. In this paper, we identified 29 ZFP genes in Gossypium hirsutum. This gene family was divided into seven subfamilies, 22 of which were distributed over 17 chromosomes. Bioinformatic analysis revealed that 20 GhZFP genes originated from whole genome duplications and two originated from dispersed duplication events, indicating that whole genome duplication is the main force in the expansion of the GhZFP gene family. Most GhZFP8 subfamily genes, except for GhZFP8–3, were highly expressed during fiber cell growth, and were induced by brassinosteroids in vitro. Furthermore, we found that a large number of GhZFP genes contained gibberellic acid responsive elements, auxin responsive elements, and E-box elements in their promoter regions. Exogenous application of these hormones significantly stimulated the expression of these genes. Our findings reveal that GhZFP8 genes are involved in cotton fiber development and widely induced by auxin, gibberellin and BR, which provides a foundation for the identification of more downstream genes with potential roles in phytohormone stimuli, and a basis for breeding better cotton varieties in the future.

Bone homeostasis is maintained through continuous remodeling by osteoclast-driven bone resorption and osteoblast-mediated bone formation. Osteoclasts are multinucleated giant cells (MNCs) differentiated from myeloid progenitors of the monocytic lineage. During osteoclast maturation, DC-STAMP (dendritic cell specific transmembrane protein) has been shown as a master determinant of osteoclast cell fusion. In this study, we demonstrate that Mex3B inhibits osteoclast fusion protein DCSTAMP expression and osteoclastogenesis. During differentiation of osteoclasts, the expression of Mex3B is down-regulated by cytokines such as RANKL and TNFa, resulting in relief of Mex3B-mediated down-regulation of DC-STAMP mRNA level. Our findings not only reveal critical mechanisms on regulation of DC-STAMP-mediated osteoclastogenesis, but also point to Mex3B as a potential therapeutic target for the treatment of human bone diseases.

Chikungunya virus (CHIKV), an enveloped positive-sense RNA virus, is a member of the alphaviruses and cause fever and arthralgia in humans. We performed genome-wide CRISPR/Cas9-based screens and identified Y-box binding protein 1 (YBX1) as an essential cellular factor for CHIKV. Deficiency of YBX1 inhibited CHIKV RNA replication and impaired virus production. Upon CHIKV infection, YBX1 showed a striking re-localization to viral replication complexes (vRCs), where it co-localized with CHIKV nsP3 and dsRNA intermediates. YBX1 directly interacted with CHIKV nsP3, and mutation of the YBX1-binding motif in CHIKV nsP3 suppressed viral replication in host cells. Furthermore, YBX1 bound to viral RNA and increased the viral RNA-binding activity of CHIKV nsP3. Consistently, the RNA-binding activity of YBX1, as well as the ability of nsP3 to bind to YBX1, was required for efficient CHIKV replication. In addition to CHIKV, YBX1 was also essential for replication of all examined alphaviruses including the prototypic alphavirus. Our findings suggest that YBX1 acts as a scaffold for assembly of chikungunya vRCs and an important factor for replication of multiple alphaviruses, which may serve as a potential target for the development of anti-alphavirus therapies. IMPORTANCE: Alphaviruses are a group of mosquito-transmitted, enveloped, positive-strand RNA viruses in the Togaviridae family. Most alphaviruses are important pathogens that continue to cause human disease ranging from severe and potentially fatal neurological disease to chronic arthritic disease on a global scale. Here, we found that YBX1 promotes binding of CHIKV genomic RNA to nsP3, which is a key component of the replication complex, and is therefore pivotal for CHIKV replication. Deficiency of YBX1 results in reduced replication of multiple alphaviruses, including arthritogenic and encephalitic alphaviruses. These findings suggest that YBX1 is an important cellular factor for multiple alphaviruses and a potential target for preventing alphavirus infections.

The change in the three-dimensional (3D) structure of a protein can affect its own function or interaction with other protein(s), which may lead to disease(s). Gene mutations, especially missense mutations, are the main cause of changes in protein structure. Due to the lack of protein crystal structure data, about three-quarters of human mutant proteins cannot be predicted or accurately predicted, and the pathogenicity of missense mutations can only be indirectly evaluated by evolutionary conservation. Recently, many computational methods have been developed to predict protein 3D structures with accuracy comparable to experiments. This progress enables the information of structural biology to be further utilized by clinicians. Thus, we developed a user-friendly platform named DPL3D (http://nsbio.tech:3000) which can predict and visualize the 3D structure of mutant proteins. The crystal structure and other information of proteins were downloaded together with the software including AlphaFold 2, RoseTTAFold, RoseTTAFold All-Atom, and trRosettaX-Single. We implemented a query module for 210,180 molecular structures, including 52,248 human proteins. Visualization of protein two-dimensional (2D) and 3D structure prediction can be generated via LiteMol automatically or manually and interactively. This platform will allow users to easily and quickly retrieve large-scale structural information for biological discovery.