Preparation and Properties of the Recombinant Tenebrio molitor SerPH122—Proteolytically Active Homolog of Serine Peptidase

Tereshchenkova, Valeriia F.; Zhiganov, N. I.; Akentyev, Philipp; Gubaidullin, I. I.; Козлов, Д. Г.; Belyaeva, N. V.; Filippova, I. Yu.; Elpidina, Elena N.

doi:10.1134/s0003683821050161

Cited by 1 publication

(3 citation statements)

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“…Note that among the highly expressed SPHs ( Table 8 ), there are SerPH122 and SerPH245 with conservative Ser/Thr substitution in the active center in contrast to the radical replacements in the other SPHs. Characterization of recombinant SerPH122 showed that this synonymous homolog had low but reliably detectable proteolytic activity towards chymotrypsin and trypsin chromogenic peptide substrates [ 33 ].…”

Section: Resultsmentioning

confidence: 99%

“…The physiological role of SPHs is still poorly understood; however, some of them highly expressed (9 out of 95) during the feeding stages may play a certain regulatory role that may be related with digestive peptidase activation or their interaction with substrates or inhibitors in the midgut lumen. It was shown that some of the homologs are able to bind with the substrates and even provide a low-rate hydrolysis [ 33 , 50 ].…”

Section: Discussionmentioning

confidence: 99%

“…Analyzing trypsin-like SPs/SPHs in transcriptome datasets from different stages of the T. molitor life cycle, we have previously de novo assembled 54 trypsins and five trypsin-like SPHs [ 31 ]. We also characterized recombinant preparations of SP, SerP38, and SPH, SerPH122, expressed in the Komagataella kurtzmanii system [ 32 , 33 ]. Recent work by Wu and coauthors [ 34 ] provided information on 200 T. molitor genes including 112 SPs and 88 SPHs, and transcriptome datasets together with RT-PCR analysis were used for SP-related genes expression profiling at various developmental stages and tissues.…”

Section: Introductionmentioning

confidence: 99%

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The Set of Serine Peptidases of the Tenebrio molitor Beetle: Transcriptomic Analysis on Different Developmental Stages

Zhiganov,

Vinokurov,

Salimgareev

et al. 2024

IJMS

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Serine peptidases (SPs) of the chymotrypsin S1A subfamily are an extensive group of enzymes found in all animal organisms, including insects. Here, we provide analysis of SPs in the yellow mealworm Tenebrio molitor transcriptomes and genomes datasets and profile their expression patterns at various stages of ontogeny. A total of 269 SPs were identified, including 137 with conserved catalytic triad residues, while 125 others lacking conservation were proposed as non-active serine peptidase homologs (SPHs). Seven deduced sequences exhibit a complex domain organization with two or three peptidase units (domains), predicted both as active or non-active. The largest group of 84 SPs and 102 SPHs had no regulatory domains in the propeptide, and the majority of them were expressed only in the feeding life stages, larvae and adults, presumably playing an important role in digestion. The remaining 53 SPs and 23 SPHs had different regulatory domains, showed constitutive or upregulated expression at eggs or/and pupae stages, participating in regulation of various physiological processes. The majority of polypeptidases were mainly expressed at the pupal and adult stages. The data obtained expand our knowledge on SPs/SPHs and provide the basis for further studies of the functions of proteins from the S1A subfamily in T. molitor.

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Section: Resultsmentioning

confidence: 99%

Section: Discussionmentioning

confidence: 99%