• Login
    View Item 
    •   Home
    • UA Graduate and Undergraduate Research
    • UA Theses and Dissertations
    • Dissertations
    • View Item
    •   Home
    • UA Graduate and Undergraduate Research
    • UA Theses and Dissertations
    • Dissertations
    • View Item
    JavaScript is disabled for your browser. Some features of this site may not work without it.

    Browse

    All of UA Campus RepositoryCommunitiesTitleAuthorsIssue DateSubmit DateSubjectsPublisherJournalThis CollectionTitleAuthorsIssue DateSubmit DateSubjectsPublisherJournal

    My Account

    LoginRegister

    About

    AboutUA Faculty PublicationsUA DissertationsUA Master's ThesesUA Honors ThesesUA PressUA YearbooksUA CatalogsUA Libraries

    Statistics

    Most Popular ItemsStatistics by CountryMost Popular Authors

    Approaches to understanding the regulation of trypsin gene expression in mosquitoes

    • CSV
    • RefMan
    • EndNote
    • BibTex
    • RefWorks
    Thumbnail
    Name:
    azu_td_3031405_sip1_m.pdf
    Size:
    2.227Mb
    Format:
    PDF
    Download
    Author
    Nussenzveig, Roberto Henrique
    Issue Date
    2001
    Keywords
    Biology, Molecular.
    Biology, Genetics.
    Chemistry, Biochemistry.
    Advisor
    Wells, Michael A.
    
    Metadata
    Show full item record
    Publisher
    The University of Arizona.
    Rights
    Copyright © is held by the author. Digital access to this material is made possible by the University Libraries, University of Arizona. Further transmission, reproduction or presentation (such as public display or performance) of protected items is prohibited except with permission of the author.
    Abstract
    In order to identify potential cis-acting elements responsible for the correct expression of the mosquito trypsin genes we have resorted to an evolutionary approach. This approach is based on the identification of DNA footprints that are conserved in homologous genes isolated from different species. Several trypsin clones have been isolated from Aedes species specific genomic DNA libraries, and by sequencing been shown to contain an ORF coding for the late trypsin gene. Analysis of the 5' FLR's of the species specific late trypsin genes, reveals the presence of a conserved TATA-box and transcriptional initiator. A phylogenetic footprinting analysis detected some evolutionarily conserved sequence elements in the 5' regulatory regions of the late trypsin gene. A cis-element that bears sequence similarity with the target of the transcription factor Tinman has been identified. Analysis of the trypsin coding region shows that the late trypsin from the most distant species retains approximately 83% amino acid identity with late trypsin from Ae aegypti. Furthermore, unique features of the late trypsin specificity pocket from Ae aegypti are retained in all species examined making this a unique evolutionary molecular tag for this serine protease. The dicotomy of a positive/negative charge observed in the specificity pocket of trypsin members of the chymotrypsin family of serine proteases is retained; however, the conserved aspartate is replaced by a glutamate. The position of this glutamate is displaced towards the N-terminus by a serine, which is characteristic of chymotrypsin-like enzymes from the same family. Moreover, there is an insertion of a proline after the serine amino acid at the C-terminal end of the pocket. Alignment of this trypsin to other members of the same protease family strongly suggests that it is related to a unique group of proteases called serine collagenases. The most important enzymatic characteristic of enzymes belonging to this group is there lack of substrate specificity. Outside of the typical metalloproteases, these are the only proteases known to cleave collagen. What these observations mean in terms of the evolution of enzyme specificity aid structural fold remain to be elucidated.
    Type
    text
    Dissertation-Reproduction (electronic)
    Degree Name
    Ph.D.
    Degree Level
    doctoral
    Degree Program
    Graduate College
    Biochemistry
    Degree Grantor
    University of Arizona
    Collections
    Dissertations

    entitlement

     
    The University of Arizona Libraries | 1510 E. University Blvd. | Tucson, AZ 85721-0055
    Tel 520-621-6442 | repository@u.library.arizona.edu
    DSpace software copyright © 2002-2017  DuraSpace
    Quick Guide | Contact Us | Send Feedback
    Open Repository is a service operated by 
    Atmire NV
     

    Export search results

    The export option will allow you to export the current search results of the entered query to a file. Different formats are available for download. To export the items, click on the button corresponding with the preferred download format.

    By default, clicking on the export buttons will result in a download of the allowed maximum amount of items.

    To select a subset of the search results, click "Selective Export" button and make a selection of the items you want to export. The amount of items that can be exported at once is similarly restricted as the full export.

    After making a selection, click one of the export format buttons. The amount of items that will be exported is indicated in the bubble next to export format.