Warning: mysql_query() [function.mysql-query]: Unable to save result set in /data/www/shop/includes/db.inc.php on line 50
Database error: Invalid SQL: select count(id) from dev_comment where pid='200222' and iffb='1'
MySQL Error: 1194 (Table 'dev_comment' is marked as crashed and should be repaired)
#0 dbbase_sql->halt(Invalid SQL: select count(id) from dev_comment where pid='200222' and iffb='1') called at [/data/www/shop/includes/db.inc.php:54] #1 dbbase_sql->query(select count(id) from {P}_comment where pid='200222' and iffb='1') called at [/data/www/shop/comment/module/CommentContent.php:65] #2 CommentContent() called at [/data/www/shop/includes/common.inc.php:551] #3 printpage() called at [/data/www/shop/comment/html/index.php:13]
Warning: mysql_fetch_array(): supplied argument is not a valid MySQL result resource in /data/www/shop/includes/db.inc.php on line 61

Warning: mysql_query() [function.mysql-query]: Unable to save result set in /data/www/shop/includes/db.inc.php on line 50
Database error: Invalid SQL: select * from dev_comment where pid='200222' and iffb='1' order by id limit 0,10
MySQL Error: 1194 (Table 'dev_comment' is marked as crashed and should be repaired)
#0 dbbase_sql->halt(Invalid SQL: select * from dev_comment where pid='200222' and iffb='1' order by id limit 0,10) called at [/data/www/shop/includes/db.inc.php:54] #1 dbbase_sql->query(select * from {P}_comment where pid='200222' and iffb='1' order by id limit 0,10) called at [/data/www/shop/comment/module/CommentContent.php:167] #2 CommentContent() called at [/data/www/shop/includes/common.inc.php:551] #3 printpage() called at [/data/www/shop/comment/html/index.php:13]
Warning: mysql_fetch_array(): supplied argument is not a valid MySQL result resource in /data/www/shop/includes/db.inc.php on line 61
网友点评--光明云南石斛商城
网站标志
导航菜单
购物车
购物车 0 件商品 | 查看购物车 | 我的订单 | 我的积分 | 会员中心
当前日期时间
当前时间:
商品搜索
商品搜索:
价格
点评详情
点评详情
发布于:2019-3-28 12:53:23  访问:8 次 回复: 篇
版主管理 | 推荐 | 删除 | 删除并扣分
S {is the|will be the|may be the|would be
This PubMed ID:https://www.ncbi.nlm.nih.gov/pubmed/27010563 suggests a function in sub-cellular localization as a GW572016 manufacturer widespread function for the PAS domain. The continued capability of YycG to localize towards the septum in depletion and deletion strains of the interacting proteins could have two motives. (1) The a lot of interactions made by fulllength Y.S is the ubiquitous function for all these domains, or irrespective of whether
S could be the ubiquitous function for all these domains, or whether other functions remain to become identified. Our data suggests that the YycG PAS domain serves as a cell-sorting module expected to direct YycG for the septum. PAS domains had been shown to be expected for localization to precise cellular compartments to get a handful of other histidine kinases (Angelastro et al., 2010; Boyd, 2000; Hallez et al., 2007). This PubMed ID:https://www.ncbi.nlm.nih.gov/pubmed/27010563 suggests a role in sub-cellular localization as a typical function for the PAS domain. While septum localization of YycG was FtsZ-dependent, a direct interaction amongst these two proteins couldn‘t be identified. A soluble construct of YycG failed to interact with FtsZ in vitro (Fukushima et al., 2008) and our two-hybrid study failed to recognize interactionsMol Microbiol. Author manuscript; readily available in PMC 2013 January 27.Fukushima et al.Pagebetween the two proteins in vivo. The two-hybrid analyses did single out quite a few divisome proteins as possible YycG interaction partners, namely DivIB, FtsL,Pbp2B and maybe FtsW. FtsL can be a short coiled-coil transmembrane spanning proteins and consists of a limited Nterminal cytoplasmic and much more comprehensive C-terminal extra-cytoplasmic portion. DivIB and Pbp2B are bigger transmembrane spanning proteins with substantial extra-cytoplasmic domains (reviewed in (Errington et al., 2003; Goehring and Beckwith, 2005)). FtsW is an integral membrane protein with 10 transmembrane helices. From the four proteins, only Pbp2B features a identified catalytic activity (transpeptidase), whereas FtsL, DivIB and FtsW are likely scaffolding proteins essential for the integrity with the divisome complex, which serves to recruit other proteins, for the septum (Errington et al., 2003; Goehring and Beckwith, 2005). A sizable physique of literature on the B. subtilis proteins and their orthologs in other bacteria (DivIB orthologs are named FtsQ in Gram-negative bacteria) has established several interactions, an interdependence for protein stability and septum place, which appear to differ slightly from 1 organism to a different (reviewed in (Errington et al., 2003; Goehring and Beckwith, 2005)). Various roles are also suggestive primarily based on the drastic distinction in protein copy numbers determined for some of these proteins in PubMed ID:https://www.ncbi.nlm.nih.gov/pubmed/27104741 E. coli (25-50 copies FtsQ, 20- 200 copies of FtsL), and B. subtilis (5000-13000 copies DivIB,) (Robichon et al., 2008; Wadsworth et al., 2008), possibly owing for the distinction in cell wall architecture between Gram-positives and Gram negatives. Our immunofluorescent experiments in strains that have been depleted for FtsL, deleted for DivIB, or depleted for FtsW demonstrated that no single one of these interacting proteins was expected for YycG localization (Fig. 6). Since the bulk of these proteins is within the membrane or the extra-cytoplasmic space, these final results are constant with our observations that cytoplasmic YycG fragments retained the ability to localize to the septum.
共篇回复 每页10篇 页次:1/1
共篇回复 每页10篇 页次:1/1
我要回复
回复内容
验 证 码
看不清?更换一张
匿名发表 
脚注信息
Copyright (C) 2015-2016 All Rights Reserved. 光明云南石斛商城管理系统 版权所有   滇ICP备11005439号-1
服务时间:周一至周日 09:00 — 18:00  全国订购及服务热线:0691-5161027 
联系地址:云南省西双版纳傣族自治州勐海县工业园区   邮政编码:666200