NDLI: Molecular mechanisms for interaction of glycine betaine with supra-molecular phycobiliprotein complexes

Content Provider	Springer Nature Link
Author	Xu, XiuLing Li, Heng Xie, Jie Zhao, JingQuan
Copyright Year	2009
Abstract	Glycine betaine (GB) is a biologically important small molecule protecting cells, proteins and enzymes in vivo and in vitro under environmental stresses. Recently, it was found that GB could also relax the structure and inactivate the function of phycobiliproteins and phycobilisome (PBS), a kind of supra-molecular complexes, in cyanobacterial cells. The molecular mechanisms for the opposite phenomena are quite ambiguous. Taking PBS and a trimeric or monomeric C-phycocyanin (C-PC) as models, the molecular mechanism for the interaction of GB with supra-molecular complexes or nuclear proteins was investigated. The energetic decoupling of PBS components induced by GB suggests that the PBS core-membrane linking polypeptide was the most sensitive site while the rod-core linker was the next. Biochemistry analysis proves that PBS structure was loosened but not dissociated into the components. On the basis of the results and structure knowledge, it was proposed that GB screened the electrostatic attraction of the opposite charges on a linker and a protein leading to a much looser structure. It was observed that GB induced a spectral blue shift for trimeric C-PC but a red shift for a monomeric C-PC (a nuclear protein), which were ascribed to GB’s screening of the electrostatic attraction of a linker to a protein and strengthening of the hydrophobic interaction between C-PC monomers. The trimers and monomers’ forming of the same products under high concentration of GB was ascribed to a compromise of the opposite interaction forces.
Starting Page	1865
Ending Page	1870
Page Count	6
File Format	PDF
ISSN	10069291
Journal	Science in China Series B: Chemistry
Volume Number	52
Issue Number	11
e-ISSN	18622771
Language	English
Publisher	SP Science in China Press
Publisher Date	2009-11-25
Publisher Place	Heidelberg
Access Restriction	Subscribed
Subject Keyword	glycine betaine phycobiliproteins phycobilisome supra-molecular complex molecular interaction mechanism Chemistry/Food Science
Content Type	Text
Resource Type	Article
Subject	Chemistry

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