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Bioinformatic Analysis of the Origins of ABCA and ABCG Families and Development of the Thermostability Assay for ABCG2.

紀錄類型:	書目-電子資源 : Monograph/item
正題名/作者:	Bioinformatic Analysis of the Origins of ABCA and ABCG Families and Development of the Thermostability Assay for ABCG2./
作者:	Balakrishnan, Abilasha.
面頁冊數:	1 online resource (172 pages)
附註:	Source: Masters Abstracts International, Volume: 83-05.
Contained By:	Masters Abstracts International83-05.
標題:	Physiology. -
電子資源:	http://pqdd.sinica.edu.tw/twdaoapp/servlet/advanced?query=28731718click for full text (PQDT)
ISBN:	9798544225485

Bioinformatic Analysis of the Origins of ABCA and ABCG Families and Development of the Thermostability Assay for ABCG2.
Balakrishnan, Abilasha.

Bioinformatic Analysis of the Origins of ABCA and ABCG Families and Development of the Thermostability Assay for ABCG2. - 1 online resource (172 pages)

Source: Masters Abstracts International, Volume: 83-05.

Thesis (M.Phil.)--The University of Manchester (United Kingdom), 2021.

Includes bibliographical references

The ATP-binding cassette super-family G member 2(ABCG2); also known as the breast cancer resistant protein) mapped on chromosome 4q22 is known to have important physiological roles in many tissues such as mammary gland, blood brain barrier and gastrointestinal tract. Furthermore, ABCG2 is involved in the transportation of chemically diverse substrates such as steroids and other organic ions. Most importantly, ABCG2 has been suggested to be involved in multidrug resistance in chemotherapy. Understanding the thermostability of the ABCG2 protein, will allow a better understanding of how drugs and inhibitor interact with the protein. The first aim in this thesis was to express, characterise and purify ABCG2 using Pichia pastoris, hence establish whether the thermostability cellular thermal shift assay (CETSA) showed proof of principle on ABCG2. Results concluded that Pichia pastoris is an excellent expression system which can be used to express and characterise ABCG2. The thermostability CETSA assay performed on ABCG2 showed that the melting temperature was 55°C, thus, proving that the CETSA assay could be used in future to examine the thermostability of ABCG2 in the presence of a ligand. Understanding the structure and mechanism of ABCG2 starts by looking at the evolutionary relationship with a common ancestor. The second aim of this thesis was to find potential evolutionary relationship between ABCA and ABCG families to bacterial ABC transporter such as: mechanotransducer MacB, WzmWzt, MlaE and MlaF. Results showed MacB transmembrane domain (TMD), and nucleotide binding domain (NBD) had significant alignment to TMD and NBD of ATP-binding cassette super-family A member 1 (ABCA1), ABCG2 and ATPbinding cassette super-family G member 5 and 8 (ABCG5/G8). Henceforth, indicating ABCA and ABCG families may have originated from MacB transporters. Similarly, the TMD and NBD of WzmWzt, MlaE and MlaF are seen to align significantly well to the TMD and NBD of ABCA and ABCG families, this suggest that convergence evolution may be taking place between the two families.

Electronic reproduction.
Ann Arbor, Mich. :
ProQuest,
2023

Mode of access: World Wide Web

ISBN: 9798544225485Subjects--Topical Terms:

518431
Physiology.
Index Terms--Genre/Form:

542853
Electronic books.

Bioinformatic Analysis of the Origins of ABCA and ABCG Families and Development of the Thermostability Assay for ABCG2.
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504 $a Includes bibliographical references
520 $a The ATP-binding cassette super-family G member 2(ABCG2); also known as the breast cancer resistant protein) mapped on chromosome 4q22 is known to have important physiological roles in many tissues such as mammary gland, blood brain barrier and gastrointestinal tract. Furthermore, ABCG2 is involved in the transportation of chemically diverse substrates such as steroids and other organic ions. Most importantly, ABCG2 has been suggested to be involved in multidrug resistance in chemotherapy. Understanding the thermostability of the ABCG2 protein, will allow a better understanding of how drugs and inhibitor interact with the protein. The first aim in this thesis was to express, characterise and purify ABCG2 using Pichia pastoris, hence establish whether the thermostability cellular thermal shift assay (CETSA) showed proof of principle on ABCG2. Results concluded that Pichia pastoris is an excellent expression system which can be used to express and characterise ABCG2. The thermostability CETSA assay performed on ABCG2 showed that the melting temperature was 55°C, thus, proving that the CETSA assay could be used in future to examine the thermostability of ABCG2 in the presence of a ligand. Understanding the structure and mechanism of ABCG2 starts by looking at the evolutionary relationship with a common ancestor. The second aim of this thesis was to find potential evolutionary relationship between ABCA and ABCG families to bacterial ABC transporter such as: mechanotransducer MacB, WzmWzt, MlaE and MlaF. Results showed MacB transmembrane domain (TMD), and nucleotide binding domain (NBD) had significant alignment to TMD and NBD of ATP-binding cassette super-family A member 1 (ABCA1), ABCG2 and ATPbinding cassette super-family G member 5 and 8 (ABCG5/G8). Henceforth, indicating ABCA and ABCG families may have originated from MacB transporters. Similarly, the TMD and NBD of WzmWzt, MlaE and MlaF are seen to align significantly well to the TMD and NBD of ABCA and ABCG families, this suggest that convergence evolution may be taking place between the two families.
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