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Cloning and analysis of pyrG gene encoding orotidine 5-Monophosphate decarboxylase of aspergillus oryzaeStrain S1

In this study, the pyrG gene which encodes for orotidine 5-monophosphate decarboxylase (OMP decarboxylase) of Aspergillus oryzae strain S1 was cloned and analysed. This 1.8kb A. oryzae pyrG encompasses the 5’-regulatory flanking region (465 bp), open reading frame (899 bp) and 3’-regulatory region (...

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Main Authors: Selina Oh Siew Ling,, Leong, Jiun Min, Abdul Munir Abdul Murad,, Nor Muhammad Mahadi,, Farah Diba Abu Bakar,
Format: Article
Language:English
Published: Universiti Kebangsaan Malaysia 2011
Online Access:http://journalarticle.ukm.my/2393/1/08_Selina.pdf
http://journalarticle.ukm.my/2393/
http://www.ukm.my/jsm/
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spelling my-ukm.journal.23932016-12-14T06:31:29Z http://journalarticle.ukm.my/2393/ Cloning and analysis of pyrG gene encoding orotidine 5-Monophosphate decarboxylase of aspergillus oryzaeStrain S1 Selina Oh Siew Ling, Leong, Jiun Min Abdul Munir Abdul Murad, Nor Muhammad Mahadi, Farah Diba Abu Bakar, In this study, the pyrG gene which encodes for orotidine 5-monophosphate decarboxylase (OMP decarboxylase) of Aspergillus oryzae strain S1 was cloned and analysed. This 1.8kb A. oryzae pyrG encompasses the 5’-regulatory flanking region (465 bp), open reading frame (899 bp) and 3’-regulatory region (475 bp). The pyrG contained one intron at position 623-687 bp based on the AUGUSTUS and FGENESH (SoftBerry) analysis corresponding to the intron present in the pyrG of A. oryzae (Accession Number: Y13811). In silico analysis showed that the enzyme encoded by the A. oryzae S1 pyrG gene has a theoretical molecular weight of 30.28 kDa and theoretical pI value of 5.92. This enzyme is hydrophilic, located in a region outside of the transmembrane and it functions in the cytoplasm. Five motives such as N-glycosylation site, protein kinase C (PKC) phosphorylation site, casein kinase II (CK-2) phosphorylation site, N-myristolation site and orotidine 5-monophoshate decarboxylase active site have been identified in the pyrG amino acid sequence. The three dimensional structure of this enzyme generated via protein homology modeling using the bioinformatic software, Swiss Model, shows that OMP decarboxylase is a protein with an α/ß barrel structure possessing 8 ß-strands surrounded by 9 α-helices. The amino acid residues involved in the active site have been identified and it is located on one of the ß-strands. The pyrG DNA sequence will be used for the complementation of a pyrG auxotroph mutant of A. oryzae. Universiti Kebangsaan Malaysia 2011-04 Article PeerReviewed application/pdf en http://journalarticle.ukm.my/2393/1/08_Selina.pdf Selina Oh Siew Ling, and Leong, Jiun Min and Abdul Munir Abdul Murad, and Nor Muhammad Mahadi, and Farah Diba Abu Bakar, (2011) Cloning and analysis of pyrG gene encoding orotidine 5-Monophosphate decarboxylase of aspergillus oryzaeStrain S1. Sains Malaysiana, 40 (4). pp. 331-337. ISSN 0126-6039 http://www.ukm.my/jsm/
institution Universiti Kebangsaan Malaysia
building Perpustakaan Tun Sri Lanang Library
collection Institutional Repository
continent Asia
country Malaysia
content_provider Universiti Kebangsaan Malaysia
content_source UKM Journal Article Repository
url_provider http://journalarticle.ukm.my/
language English
description In this study, the pyrG gene which encodes for orotidine 5-monophosphate decarboxylase (OMP decarboxylase) of Aspergillus oryzae strain S1 was cloned and analysed. This 1.8kb A. oryzae pyrG encompasses the 5’-regulatory flanking region (465 bp), open reading frame (899 bp) and 3’-regulatory region (475 bp). The pyrG contained one intron at position 623-687 bp based on the AUGUSTUS and FGENESH (SoftBerry) analysis corresponding to the intron present in the pyrG of A. oryzae (Accession Number: Y13811). In silico analysis showed that the enzyme encoded by the A. oryzae S1 pyrG gene has a theoretical molecular weight of 30.28 kDa and theoretical pI value of 5.92. This enzyme is hydrophilic, located in a region outside of the transmembrane and it functions in the cytoplasm. Five motives such as N-glycosylation site, protein kinase C (PKC) phosphorylation site, casein kinase II (CK-2) phosphorylation site, N-myristolation site and orotidine 5-monophoshate decarboxylase active site have been identified in the pyrG amino acid sequence. The three dimensional structure of this enzyme generated via protein homology modeling using the bioinformatic software, Swiss Model, shows that OMP decarboxylase is a protein with an α/ß barrel structure possessing 8 ß-strands surrounded by 9 α-helices. The amino acid residues involved in the active site have been identified and it is located on one of the ß-strands. The pyrG DNA sequence will be used for the complementation of a pyrG auxotroph mutant of A. oryzae.
format Article
author Selina Oh Siew Ling,
Leong, Jiun Min
Abdul Munir Abdul Murad,
Nor Muhammad Mahadi,
Farah Diba Abu Bakar,
spellingShingle Selina Oh Siew Ling,
Leong, Jiun Min
Abdul Munir Abdul Murad,
Nor Muhammad Mahadi,
Farah Diba Abu Bakar,
Cloning and analysis of pyrG gene encoding orotidine 5-Monophosphate decarboxylase of aspergillus oryzaeStrain S1
author_facet Selina Oh Siew Ling,
Leong, Jiun Min
Abdul Munir Abdul Murad,
Nor Muhammad Mahadi,
Farah Diba Abu Bakar,
author_sort Selina Oh Siew Ling,
title Cloning and analysis of pyrG gene encoding orotidine 5-Monophosphate decarboxylase of aspergillus oryzaeStrain S1
title_short Cloning and analysis of pyrG gene encoding orotidine 5-Monophosphate decarboxylase of aspergillus oryzaeStrain S1
title_full Cloning and analysis of pyrG gene encoding orotidine 5-Monophosphate decarboxylase of aspergillus oryzaeStrain S1
title_fullStr Cloning and analysis of pyrG gene encoding orotidine 5-Monophosphate decarboxylase of aspergillus oryzaeStrain S1
title_full_unstemmed Cloning and analysis of pyrG gene encoding orotidine 5-Monophosphate decarboxylase of aspergillus oryzaeStrain S1
title_sort cloning and analysis of pyrg gene encoding orotidine 5-monophosphate decarboxylase of aspergillus oryzaestrain s1
publisher Universiti Kebangsaan Malaysia
publishDate 2011
url http://journalarticle.ukm.my/2393/1/08_Selina.pdf
http://journalarticle.ukm.my/2393/
http://www.ukm.my/jsm/
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score 13.211869

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