## 1 Introduction  
Tubulin is a cytoskeletal polymer formed by the assemblage of heterodimers, including \(\alpha\)-tubulin and \(\beta\)-tubulin. Tubulin multi-protein superfamily members comprise functionally distinct subtypes: a, \(b,g,d,e,z\), \(h,q\), and \(t\). Based on their inherent functional domains, \(\alpha\)-tubulin and \(\beta\)-tubulin are classified as N-terminal, middle, and C-terminal \(a/b\) tubulin domain proteins [1]. Additional studies have reclassified C-terminal tubulin domain-containing proteins into six subgroups based on the amino acid composition of the conserved functional domain, with the amino acid sequences of C-terminal \(\alpha\)- and \(\beta\)-tubulin domain from the same species sharing a high identity. For instance, studies showed that sequences of the C-terminal \(\alpha\)- and \(\beta\)-tubulin domain proteins from mice shared up to 91-100% [2]. In addition, the terminal structure interacts with tubulin-related protein MAPs to regulate tubulin assembly [3]. Mechanistically, some chaperones and protein cofactors play significant roles in modulating the proper folding of \(\alpha/\beta\)-tubulin heterodimers. Studies have shown that stable interactions between the tubulin-binding cofactor (TBC) and synthesized polypeptides of tubulin bonded to cytosolic chaperones facilitate the proper folding of tubulin proteins [4]. Tubulin binding cofactor C (TBCC) is an essential protein for the correct folding of \(\alpha\)- and \(\beta\)-tubulin and their polymerization into microtubule heterodimers [5]. Research demonstrations have shown that the five types of tubulin-binding factors (TBCS) modulate the progression of vital cellular and physiological processes by exerting direct regulatory roles in tubulin synthesis and the polymerization of microtubules [6]. TBCC dysfunction triggers the development of neurological diseases [7]. Additional research has shown that the TBCC-dependent regulation of GTPase activity and the mediation of native tubulin folding exert significant inhibitory effects on tumor and breast cancer cells [8; 9]. In humans, tubulin-binding cofactor C (TBCC) represents a post-chaperone binding protein that essentially promotes the proper folding and assemblage of \(\alpha\)- and \(\beta\)-tubulin monomers and the efficient formation of tubulin heterodimers and results in the regulation of microtubule polymerization [10]. NMR spectroscopy-based research investigations revealed the location of TBCC at the centrosome and also confirmed the existence of physical interactions between dimers of N-terminal domain-containing \(\alpha/\beta\)-tubulin proteins and TBCC [11]. The subsequent treatment of HeLa cell cultures with TBCC RNAi revealed a significant depletion in TBCC, resulting in multipolar spindles and mitotic failure, underscoring the role of TBCC in bipolar spindle formation [12]. The tubulin-specific chaperone cofactor C regulates retinitis pigmentosa 2 [10]. Although the impact of tubulin-mediated regulation of cellular processes, including trafficking, cell division, cell morphogenesis, organelle positioning, cell migration, and polarity, on diverse developmental transformations in different organisms has been demonstrated [13], the direct and indirect influence of TBC and tubulin on the morphological and pathological development of _P. capsaicin_ and other economically crucial phytopathogeniceomycetes are still unknown. In the current study, we identified nine TBC domain-containing proteins in _P. capsaicin_, the causal agent of foliar blight, damping-off, wilting, and root, stem, and fruit rot disease in more 45 fruits and vegetable crops--including pepper (_Capsicum autumn_), tomato (_Solanum Iycopersicum_), kidney bean (_Phaseolus vulgaris_), eggplant (_Solanum melongena_), faba bean (_Vicia fiba_), watermelon, (_Citrullus lanatus_), and squash (_Cucurbita moschata_), among others. We monitored the transcriptomic dynamics of TBC-coding genes during the early and late stages of _P.