Tags

Type your tag names separated by a space and hit enter

Characterization of the molecular features and expression patterns of two serine proteases in Hermetia illucens (Diptera: Stratiomyidae) larvae.
BMB Rep. 2011 Jun; 44(6):387-92.BR

Abstract

To investigate the molecular scavenging capabilities of the larvae of Hermetia illucens, two serine proteases (SPs) were cloned and characterized. Multiple sequence alignments and phylogenetic tree analysis of the deduced amino acid sequences of Hi-SP1 and Hi-SP2 were suggested that Hi-SP1 may be a chymotrypsin- and Hi-SP2 may be a trypsin-like protease. Hi-SP1 and Hi-SP2 3-D homology models revealed that a catalytic triad, three disulfide bonds, and a substrate-binding pocket were highly conserved, as would be expected of a SP. E. coli expressed Hi-SP1 and Hi-SP2 showed chymotrypsin or trypsin activities, respectively. Hi-SP2 mRNAs were consistently expressed during larval development. In contrast, the expression of Hi-SP1 mRNA fluctuated between feeding and molting stages and disappeared at the pupal stages. These expression pattern differences suggest that Hi-SP1 may be a larval specific chymotrypsin-like protease involved with food digestion, while Hi-SP2 may be a trypsin-like protease with diverse functions at different stages.

Authors+Show Affiliations

National Academy of Agricultural Science, Rural Development Administration, Suwon, Korea.No affiliation info availableNo affiliation info availableNo affiliation info availableNo affiliation info availableNo affiliation info availableNo affiliation info availableNo affiliation info availableNo affiliation info available

Pub Type(s)

Journal Article
Research Support, Non-U.S. Gov't

Language

eng

PubMed ID

21699751

Citation

Kim, Wontae, et al. "Characterization of the Molecular Features and Expression Patterns of Two Serine Proteases in Hermetia Illucens (Diptera: Stratiomyidae) Larvae." BMB Reports, vol. 44, no. 6, 2011, pp. 387-92.
Kim W, Bae S, Kim A, et al. Characterization of the molecular features and expression patterns of two serine proteases in Hermetia illucens (Diptera: Stratiomyidae) larvae. BMB Rep. 2011;44(6):387-92.
Kim, W., Bae, S., Kim, A., Park, K., Lee, S., Choi, Y., Han, S., Park, Y., & Koh, Y. (2011). Characterization of the molecular features and expression patterns of two serine proteases in Hermetia illucens (Diptera: Stratiomyidae) larvae. BMB Reports, 44(6), 387-92. https://doi.org/10.5483/BMBRep.2011.44.6.387
Kim W, et al. Characterization of the Molecular Features and Expression Patterns of Two Serine Proteases in Hermetia Illucens (Diptera: Stratiomyidae) Larvae. BMB Rep. 2011;44(6):387-92. PubMed PMID: 21699751.
* Article titles in AMA citation format should be in sentence-case
TY - JOUR T1 - Characterization of the molecular features and expression patterns of two serine proteases in Hermetia illucens (Diptera: Stratiomyidae) larvae. AU - Kim,Wontae, AU - Bae,Sungwoo, AU - Kim,Ayoung, AU - Park,Kwanho, AU - Lee,Sangbeom, AU - Choi,Youngcheol, AU - Han,Sangmi, AU - Park,Younghan, AU - Koh,Youngho, PY - 2011/6/25/entrez PY - 2011/6/28/pubmed PY - 2011/10/21/medline SP - 387 EP - 92 JF - BMB reports JO - BMB Rep VL - 44 IS - 6 N2 - To investigate the molecular scavenging capabilities of the larvae of Hermetia illucens, two serine proteases (SPs) were cloned and characterized. Multiple sequence alignments and phylogenetic tree analysis of the deduced amino acid sequences of Hi-SP1 and Hi-SP2 were suggested that Hi-SP1 may be a chymotrypsin- and Hi-SP2 may be a trypsin-like protease. Hi-SP1 and Hi-SP2 3-D homology models revealed that a catalytic triad, three disulfide bonds, and a substrate-binding pocket were highly conserved, as would be expected of a SP. E. coli expressed Hi-SP1 and Hi-SP2 showed chymotrypsin or trypsin activities, respectively. Hi-SP2 mRNAs were consistently expressed during larval development. In contrast, the expression of Hi-SP1 mRNA fluctuated between feeding and molting stages and disappeared at the pupal stages. These expression pattern differences suggest that Hi-SP1 may be a larval specific chymotrypsin-like protease involved with food digestion, while Hi-SP2 may be a trypsin-like protease with diverse functions at different stages. SN - 1976-670X UR - https://www.unboundmedicine.com/medline/citation/21699751/Characterization_of_the_molecular_features_and_expression_patterns_of_two_serine_proteases_in_Hermetia_illucens__Diptera:_Stratiomyidae__larvae_ L2 - http://www.bmbreports.org/journal/view.html?volume=44&number=6&spage=387 DB - PRIME DP - Unbound Medicine ER -