Khan Muhammad Farhan, Parveen Shakeela, Sultana Mehwish, Zhu Peng, Xu Youhou, Safdar Areeba, Shafique Laiba
Guangxi Key Laboratory of Beibu Gulf Marine Biodiversity Conservation, Beibu Gulf University, Guangxi, 535011, People's Republic of China.
Department of Chemistry, Gomal University, Dera Ismail Khan, 29050, Pakistan.
Mol Biotechnol. 2024 Sep 6. doi: 10.1007/s12033-024-01263-x.
The members of the transforming growth factor β (TGF-β) family of cell signaling polypeptides have garnered a great deal of interest due to its capacity from nematodes to mammals to regulate cell-based activities which control the growth of embryos and sustain tissue homeostasis. The current study designed a computational analysis of the TGF-β protein family for understanding these proteins at the molecular level. This study determined the genomic structure of TGF-β gene family in Nile tilapia for the first time. We chose 33 TGF-β genes for identification and divided them into two subgroups, TGF-like and BMP-like. Moreover, the subcellular localization of the Nile tilapia TGF-β proteins have showed that majority of the members of TGF-β proteins family are present into extracellular matrix and plasma except BMP6, BMP7, and INHAC. All TGF-β proteins were thermostable excluding BMP1. Each protein exhibited basic nature, excluding of BMP1, BMP2, BMP7, BMP10, GDF2, GDF8, GDF11, AMH, INHA, INHBB, and NODAL M. All proteins gave impression of being unstable depending on the instability index, having values exceeding 40 excluding BMP1 and BMP2. Each TGF-β protein was found to be hydrophobic with lowered values of GRAVY. Moreover, every single one of the discovered TGF-β genes had a consistent evolutionary pattern. The TGF-β gene family had eight segmental duplications, and the Ka/Ks ratio demonstrated that purifying selection had an impact on the duplicated gene pairs which have experienced selection pressure. This study highlights important functionality of TGF-β and depicts the demand for further investigation to better understand the role and mechanism of transforming growth factor β in fishes and other species.
细胞信号传导多肽的转化生长因子β(TGF-β)家族成员因其从线虫到哺乳动物调节基于细胞的活动的能力而备受关注,这些活动控制胚胎的生长并维持组织稳态。当前的研究设计了对TGF-β蛋白家族的计算分析,以在分子水平上理解这些蛋白质。本研究首次确定了尼罗罗非鱼中TGF-β基因家族的基因组结构。我们选择了33个TGF-β基因进行鉴定,并将它们分为两个亚组,即TGF样和BMP样。此外,尼罗罗非鱼TGF-β蛋白的亚细胞定位表明,除BMP6、BMP7和INHAC外,TGF-β蛋白家族的大多数成员存在于细胞外基质和血浆中。除BMP1外,所有TGF-β蛋白都具有热稳定性。除BMP1、BMP2、BMP7、BMP10、GDF2、GDF8、GDF11、AMH、INHA、INHBB和NODAL M外,每种蛋白质都表现出碱性。根据不稳定指数,所有蛋白质都给人不稳定的印象,其值超过40,BMP1和BMP2除外。发现的每个TGF-β蛋白都具有较低的GRAVY值,表现为疏水性。此外,每个发现的TGF-β基因都有一致的进化模式。TGF-β基因家族有8个片段重复,Ka/Ks比率表明纯化选择对经历选择压力的重复基因对有影响。本研究突出了TGF-β的重要功能,并描述了进一步研究以更好地理解转化生长因子β在鱼类和其他物种中的作用和机制的必要性。