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Structure, Evolution and Engineering...

Scholl, Connor L.,

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Structure, Evolution and Engineering of Polyproline Type II Helical Antifreeze Proteins /

Record Type:	Electronic resources : Monograph/item
Title/Author:	Structure, Evolution and Engineering of Polyproline Type II Helical Antifreeze Proteins // Connor L Scholl.
Author:	Scholl, Connor L.,
Description:	1 electronic resource (164 pages)
Notes:	Source: Dissertations Abstracts International, Volume: 85-03, Section: B.
Contained By:	Dissertations Abstracts International85-03B.
Subject:	Cold. -
Online resource:	https://pqdd.sinica.edu.tw/twdaoapp/servlet/advanced?query=30565958
ISBN:	9798380266109

Structure, Evolution and Engineering of Polyproline Type II Helical Antifreeze Proteins /
Scholl, Connor L.,

Structure, Evolution and Engineering of Polyproline Type II Helical Antifreeze Proteins /Connor L Scholl. - 1 electronic resource (164 pages)

Source: Dissertations Abstracts International, Volume: 85-03, Section: B.

Antifreeze proteins (AFPs) bind to ice crystals to prevent organisms from freezing. A diversity of AFP folds has been found in fish and insects, including isolated and bundled alpha helices, globular proteins, and several different beta solenoids. But the variety of AFPs in flightless arthropods, like Collembola, had not been adequately assessed. In this study, antifreeze activity was shown to be present in 18 of the 22 species of Collembola from cold or temperate zones. A range of methods was used to characterize these AFPs, including isolation by ice affinity purification, MALDI mass spectrometry, amino acid composition analysis, tandem mass spectrometry sequencing, transcriptome sequencing, and bioinformatic investigations of sequence databases. All of these collembolan AFPs had a high glycine content, a common tripeptide repeat, and were predicted to have the same polyproline type II helical bundle fold, consisting of two antiparallel layers of parallel helices, with variation in the length and number of helices. To help confirm this expectation the 9-kDa AFP from the Collembola, Granisotoma rainieri, was recombinantly expressed and its X-ray crystal structure solved to 1.21-A resolution. Four of the nine polyproline type II helices in GrAFP form the ice-binding site supported by five helices on the other more hydrophilic side. This unique fold provided the opportunity to alter the ice-binding site area to explore how this affects antifreeze activity. A GrAFP construct with only three helices on the ice-binding site lost 90% of its activity. Whereas expansion to five helices produced a 3-fold increase in activity. The polyproline type II helical bundle AFP fold is unique to Collembola, and its prevalence within this class suggests it is ancient. Collembola arose in the Paleozoic Era with the two orders known to produce AFPs diverging around 400 million years ago during the Andean-Saharan Ice Age. Therefore, it is likely that the AFP arose then and persisted in many lineages through the following two ice ages and intervening warm periods, unlike the AFPs of fish, which arose independently in many taxa during the Cenozoic Ice Age beginning ~30 million years ago.

English

ISBN: 9798380266109Subjects--Topical Terms:

560283
Cold.

Structure, Evolution and Engineering of Polyproline Type II Helical Antifreeze Proteins /
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245 1 0 $a Structure, Evolution and Engineering of Polyproline Type II Helical Antifreeze Proteins / $c Connor L Scholl.
264 1 $a Ann Arbor : $b ProQuest Dissertations & Theses, $c 2023
300 $a 1 electronic resource (164 pages)
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500 $a Source: Dissertations Abstracts International, Volume: 85-03, Section: B.
500 $a Advisors: Davies, Peter L.
502 $b Ph.D. $c Queen's University (Canada) $d 2023.
520 $a Antifreeze proteins (AFPs) bind to ice crystals to prevent organisms from freezing. A diversity of AFP folds has been found in fish and insects, including isolated and bundled alpha helices, globular proteins, and several different beta solenoids. But the variety of AFPs in flightless arthropods, like Collembola, had not been adequately assessed. In this study, antifreeze activity was shown to be present in 18 of the 22 species of Collembola from cold or temperate zones. A range of methods was used to characterize these AFPs, including isolation by ice affinity purification, MALDI mass spectrometry, amino acid composition analysis, tandem mass spectrometry sequencing, transcriptome sequencing, and bioinformatic investigations of sequence databases. All of these collembolan AFPs had a high glycine content, a common tripeptide repeat, and were predicted to have the same polyproline type II helical bundle fold, consisting of two antiparallel layers of parallel helices, with variation in the length and number of helices. To help confirm this expectation the 9-kDa AFP from the Collembola, Granisotoma rainieri, was recombinantly expressed and its X-ray crystal structure solved to 1.21-A resolution. Four of the nine polyproline type II helices in GrAFP form the ice-binding site supported by five helices on the other more hydrophilic side. This unique fold provided the opportunity to alter the ice-binding site area to explore how this affects antifreeze activity. A GrAFP construct with only three helices on the ice-binding site lost 90% of its activity. Whereas expansion to five helices produced a 3-fold increase in activity. The polyproline type II helical bundle AFP fold is unique to Collembola, and its prevalence within this class suggests it is ancient. Collembola arose in the Paleozoic Era with the two orders known to produce AFPs diverging around 400 million years ago during the Andean-Saharan Ice Age. Therefore, it is likely that the AFP arose then and persisted in many lineages through the following two ice ages and intervening warm periods, unlike the AFPs of fish, which arose independently in many taxa during the Cenozoic Ice Age beginning ~30 million years ago.
546 $a English
590 $a School code: 0283
650 4 $a Cold. $3 560283
650 4 $a Glycoproteins. $3 667972
650 4 $a Ions. $3 814923
650 4 $a Nuclear magnetic resonance--NMR. $3 3560258
650 4 $a Binding sites. $3 3560349
650 4 $a Bacteria. $3 550366
650 4 $a Adsorption. $3 580046
650 4 $a Amino acids. $3 558768
650 4 $a Arthropods. $3 3689270
650 4 $a Genes. $3 600676
650 4 $a Ice. $3 566597
650 4 $a Mass spectrometry. $3 551172
650 4 $a Algae. $3 546231
650 4 $a Insects. $3 516323
650 4 $a Taxonomy. $3 3556303
650 4 $a Engineering. $3 586835
650 4 $a Microorganisms. $3 666946
650 4 $a Crystallography. $3 518393
650 4 $a Fish. $3 3564374
650 4 $a Analytical chemistry. $3 3168300
650 4 $a Chemistry. $3 516420
650 4 $a Medical imaging. $3 3172799
650 4 $a Microbiology. $3 536250
690 $a 0537
690 $a 0486
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710 2 $a Queen's University (Canada). $e degree granting institution. $3 3765623
720 1 $a Davies, Peter L. $e degree supervisor.
773 0 $t Dissertations Abstracts International $g 85-03B.
790 $a 0283
791 $a Ph.D.
792 $a 2023
856 4 0 $u https://pqdd.sinica.edu.tw/twdaoapp/servlet/advanced?query=30565958