Severity: Warning
Message: file_get_contents(https://...@pubfacts.com&api_key=b8daa3ad693db53b1410957c26c9a51b4908&a=1): Failed to open stream: HTTP request failed! HTTP/1.1 429 Too Many Requests
Filename: helpers/my_audit_helper.php
Line Number: 176
Backtrace:
File: /var/www/html/application/helpers/my_audit_helper.php
Line: 176
Function: file_get_contents
File: /var/www/html/application/helpers/my_audit_helper.php
Line: 250
Function: simplexml_load_file_from_url
File: /var/www/html/application/helpers/my_audit_helper.php
Line: 1034
Function: getPubMedXML
File: /var/www/html/application/helpers/my_audit_helper.php
Line: 3152
Function: GetPubMedArticleOutput_2016
File: /var/www/html/application/controllers/Detail.php
Line: 575
Function: pubMedSearch_Global
File: /var/www/html/application/controllers/Detail.php
Line: 489
Function: pubMedGetRelatedKeyword
File: /var/www/html/index.php
Line: 316
Function: require_once
The effects of glycerol and high temperatures on structure and function of phycobilisomes (PBSs) in vivo were investigated in a chlL deletion mutant of the cyanobacterium Synechocystis sp. PCC 6803. When the mutant was grown under light-activated heterotrophic growth conditions, it contained intact and functional PBSs, but essentially no chlorophyll and photosystems. So the structural and functional changes of the mutant PBSs in vivo can be handily detected by measurement of low temperature (77 K) fluorescence emission spectra. High concentration glycerol induced an obvious disassembly of PBSs and the dissociation of phycocyanins in the rod substructures into their oligomers and monomers. PBSs also disassembled at high temperatures and allophycocyanins were more sensitive to heat stress than phycocyanins. Our results demonstrate that the chlL(-) mutant strain is an advantageous model for studying the mechanisms of assembly and disassembly of protein complexes in vivo.
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Source |
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http://dx.doi.org/10.1016/s0014-5793(03)00973-6 | DOI Listing |
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