NDLI: Subcellular localization of the homocitrate synthase in Penicillium chrysogenum

Content Provider	Springer Nature Link
Author	Bañuelos, O. Casqueiro, J. Steidl, S. Gutiérrez, S. Brakhage, A. Martín, J.
Copyright Year	2001
Abstract	There are conflicting reports regarding the cellular localization in Saccharomyces cerevisiae and filamentous fungi of homocitrate synthase, the first enzyme in the lysine biosynthetic pathway. The homocitrate synthase (HS) gene (lys1) of Penicillium chrysogenum was disrupted in three transformants (HS–) of the Wis 54-1255 pyrG strain. The three mutants named HS1–, HS2– and HS3– all lacked homocitrate synthase activity and showed lysine auxotrophy, indicating that there is a single gene for homocitrate synthase in P. chrysogenum. The lys1 ORF was fused in frame to the gene for the green fluorescent protein (GFP) gene of the jellyfish Aequorea victoria. Homocitrate synthase-deficient mutants transformed with a plasmid containing the lys1-GFP fusion recovered prototrophy and showed similar levels of homocitrate synthase activity to the parental strain Wis 54-1255, indicating that the hybrid protein retains the biological function of wild-type homocitrate synthase. Immunoblotting analysis revealed that the HS-GFP fusion protein is maintained intact and does not release the GFP moiety. Fluorescence microscopy analysis of the transformants showed that homocitrate synthase was mainly located in the cytoplasm in P. chrysogenum; in S. cerevisiae the enzyme is targeted to the nucleus. The control nuclear protein StuA was properly targeted to the nucleus when the StuA (targeting domain)-GFP hybrid protein was expressed in P. chrysogenum. The difference in localization of homocitrate synthase between P. chrysogenum and S. cerevisiae suggests that this protein may play a regulatory function, in addition to its catalytic function, in S. cerevisiae but not in P. chrysogenum.
Starting Page	711
Ending Page	719
Page Count	9
File Format	PDF
ISSN	16174615
Journal	Molecular and General Genetics MGG
Volume Number	266
Issue Number	5
e-ISSN	16174623
Language	English
Publisher	Springer-Verlag
Publisher Date	2001-11-07
Publisher Place	Berlin/Heidelberg
Access Restriction	One Nation One Subscription (ONOS)
Content Type	Text
Resource Type	Article
Subject	Genetics Medicine Molecular Biology

Sl.	Authority	Responsibilities	Communication Details
1	Ministry of Education (GoI), Department of Higher Education	Sanctioning Authority	https://www.education.gov.in/ict-initiatives
2	Indian Institute of Technology Kharagpur	Host Institute of the Project: The host institute of the project is responsible for providing infrastructure support and hosting the project	https://www.iitkgp.ac.in
3	National Digital Library of India Office, Indian Institute of Technology Kharagpur	The administrative and infrastructural headquarters of the project	Dr. B. Sutradhar bsutra@ndl.gov.in
4	Project PI / Joint PI	Principal Investigator and Joint Principal Investigators of the project	Dr. B. Sutradhar bsutra@ndl.gov.in Prof. Saswat Chakrabarti will be added soon
5	Website/Portal (Helpdesk)	Queries regarding NDLI and its services	support@ndl.gov.in
6	Contents and Copyright Issues	Queries related to content curation and copyright issues	content@ndl.gov.in
7	National Digital Library of India Club (NDLI Club)	Queries related to NDLI Club formation, support, user awareness program, seminar/symposium, collaboration, social media, promotion, and outreach	clubsupport@ndl.gov.in
8	Digital Preservation Centre (DPC)	Assistance with digitizing and archiving copyright-free printed books	dpc@ndl.gov.in
9	IDR Setup or Support	Queries related to establishment and support of Institutional Digital Repository (IDR) and IDR workshops	idr@ndl.gov.in

Homocitrate synthase from Penicillium chrysogenum. Localization, purification of the cytosolic isoenzyme, and sensitivity to lysine.

Functional analysis and subcellular localization of two geranylgeranyl diphosphate synthases from Penicillium paxilli

Inhibition and repression of homocitrate synthase by lysine in Penicillium chrysogenum.

Inhibition and repression of homocitrate synthase by lysine in Penicillium chrysogenum.

Overexpression of the lys1 gene in Penicillium chrysogenum: homocitrate synthase levels, α-aminoadipic acid pool and penicillin production

Overexpression of the lys1 gene in Penicillium chrysogenum: homocitrate synthase levels, α-aminoadipic acid pool and penicillin production

Purification and characterization of the cold-active alkaline protease from marine cold-adaptive Penicillium chrysogenum FS010

Localization of the pathway of the penicillin biosynthesis in Penicillium chrysogenum.

Expression and tissue and subcellular localization of anthocyanidin synthase (ANS) in grapevine

Subcellular localization of the homocitrate synthase in Penicillium chrysogenum

Similar Documents

Homocitrate synthase from Penicillium chrysogenum. Localization, purification of the cytosolic isoenzyme, and sensitivity to lysine.

Functional analysis and subcellular localization of two geranylgeranyl diphosphate synthases from Penicillium paxilli

Inhibition and repression of homocitrate synthase by lysine in Penicillium chrysogenum.

Inhibition and repression of homocitrate synthase by lysine in Penicillium chrysogenum.

Overexpression of the lys1 gene in Penicillium chrysogenum: homocitrate synthase levels, α-aminoadipic acid pool and penicillin production

Overexpression of the lys1 gene in Penicillium chrysogenum: homocitrate synthase levels, α-aminoadipic acid pool and penicillin production

Purification and characterization of the cold-active alkaline protease from marine cold-adaptive Penicillium chrysogenum FS010

Localization of the pathway of the penicillin biosynthesis in Penicillium chrysogenum.

Expression and tissue and subcellular localization of anthocyanidin synthase (ANS) in grapevine

Subcellular localization of the homocitrate synthase in Penicillium chrysogenum