Abstract
SBT (Subtilisin-like serine protease), a clan of serine proteolytic enzymes, plays a versatile role in plant growth and defense. Although SBT family genes have been obtained from studies of dicots such as Arabidopsis, little is known about the potential functions of SBT in the monocots. In this study, 54 pineapple SBT genes (AcoSBTs) were divided into six subfamilies and then identified to be experienced strong purifying selective pressure and distributed on 25 chromosomes unevenly. Cis-acting element analysis indicated that almost all AcoSBTs promoters contain light-responsive elements. Further, the expression pattern via RNA-seq data showed that different AcoSBTs were preferentially expressed in different above-ground tissues. Transient expression in tobacco showed that AcoSBT1.12 was located in the plasma membrane. Moreover, Transgenic Arabidopsis ectopically overexpressing AcoSBT1.12 exhibited delayed flowering time. In addition, under the guidance of bioinformatic prediction, we found that AcoSBT1.12 could interact with AcoCWF19L, AcoPUF2, AcoCwfJL, Aco012905, and AcoSZF1 by yeast-two hybrid (Y2H). In summary, this study provided valuable information on pineapple SBT genes and illuminated the biological function of AcoSBT1.12 in floral transition.
Highlights
The normal function of plant cells is guaranteed by the precise regulation of protein level, which depends on the balance between protein synthesis and degradation (Schaller, 2004)
54 AcoSBTs were identified via the Hidden Markov Model (HMM)-based method in the pineapple genome
The expression pattern analysis showed that the expression patterns of AcoSBT genes showed an organ-specific tendency (Figures 5, 6), which is consistent with the previous findings in Arabidopsis and rice
Summary
The normal function of plant cells is guaranteed by the precise regulation of protein level, which depends on the balance between protein synthesis and degradation (Schaller, 2004). In order to ensure precise protein levels, a considerable number of limited proteases were widely distributed in plant cells. SBTs own a highly conserved domain, named Peptidase_S8 domain (PF00082), which consists of a catalytic triad with the specific arrangement of three amino acid residues (Asp, His, and Ser) (Reichardt et al, 2018). This unique domain is served as the site of specific substrate binding (Schaller et al, 2018). The conserved domains of SBTs are closely related to their versatile function evolved in plants
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