Piggy-backing the bacterial chromosome: positioning of protein complexes by chromosome segregation
Piggy-backing the bacterial chromosome: positioning of protein complexes by chromosome segregation
批准号:
BB/L002507/1
负责人:
Judith Armitage
金额:
$44.1万
依托单位:
依托单位国家:
英国
项目类别:
Research Grant
财政年份:
2013
资助国家:
英国
项目状态:
已结题
起止时间:
2013 至 --
中文摘要
当细胞分裂时,一般来说,它会产生一个合理的自我复制。随着细胞的生长,它会产生新的蛋白质,因此,在分裂之前,我们有理由认为它的蛋白质是最初细胞的两倍。当细胞分裂时,每个女儿都需要一条染色体来制造这些蛋白质,但这些蛋白质只是在子细胞之间随机分配的免费汤吗?这可能是某些蛋白质的情况,但其他蛋白质需要与伙伴蛋白质以正确的比例分开才能发挥作用。这可以通过使紧密、稳定的复合体分开来实现,但其他蛋白质组需要机制来确保每个子细胞以正确的比例拥有正确的蛋白质。长期以来,膜一直被认为是允许蛋白质聚集在一起的框架,将对外部世界变化做出反应的受体蛋白质组织成相互作用的蛋白质复合体。如果蛋白质是可溶的,不会对外部环境做出反应--它们是如何组织的,细胞如何确保子代细胞继承合适数量的复合体。最近人们意识到,在细菌细胞中,一些蛋白质复合体可以“搭载”在复制和分离的染色体上,蛋白质松散地覆盖在染色体表面,并与蛋白质复合体相互作用。当染色体分离时,这种蛋白质将这种大的蛋白质“货物”带到子细胞。这种与染色体松散相关的蛋白质与已知的蛋白质有关,这些蛋白质也确保子代细胞继承正确的遗传物质,现在很明显,细菌使用这一系统来分离以正确比例正常运作所需的广泛的蛋白质复合体。由于这是细菌中的一个共同系统,它可以被利用来组织细菌之间的其他蛋白质复合体。在许多代谢途径中,当蛋白质紧密结合时,可以实现高效率,确保局部高浓度和快速底物转移。如果这些途径在外来系统中表达,蛋白质通常会扩散和无序,导致低效率的活动率。此外,许多蛋白质与配对蛋白质一起发挥作用,为了了解它们的理想工作原理,需要确定结合时的结构特征,但通常蛋白质是单独纯化和混合的,或者当单独表达时,它们是不溶的。我们有可能利用这一自然系统来分离蛋白质复合体,以使其他蛋白质保持在功能复合体中,并保持较高的局部浓度。使用这个简化的系统,我们可以在合成生物学中使用该系统,允许子细胞以功能但高比率的方式分离蛋白质,从而有效地产生所需的产品,或者它将允许蛋白质伙伴在允许其分离和结构分析的环境中表达。为了能够利用这一新发现的机制,我们需要了解将蛋白质作为复合体连接在一起的基本成分,导致蛋白质复合体复制以及与染色体相关蛋白上的染色体的关联。
英文摘要
When a cell divides, in general it produces a reasonable replica of itself. As the cell grows it makes new proteins, so that, before division it is reasonable to assume it has twice as many proteins as the initial cell. When that cell divides each daughter needs a chromosome to make those proteins, but are the proteins just a free soup that gets randomly divided between the daughter cells? That may be the case for some proteins, but other proteins need to be divided with partner proteins in the right ratio to work. This can be done by making tight, stable complexes that get divided together, but other groups of proteins need mechanisms that ensure each daughter cell has the correct proteins in the correct ratio. Membranes have long been know to be provide a framework for allowing proteins to come together, organising receptor proteins that respond to changes in the external world into interacting protein complexes. What about proteins that are soluble and do not respond to the external environment-how to they organise and how do cells ensure daughter cells inherit the right number of complexes. It has recently been realised that in bacterial cells some protein complexes can "piggy-back" on the duplicated and segregating chromosomes, with a protein loosely covering the chromosome surface and also interacting with a complex of proteins. As the chromosome segregates this protein carries this large protein "cargo" to the daughter cell. The protein which loosely associates with the chromosome is related to proteins known to also ensure daughter cells inherit the right genetic material and it is now clear that bacteria use this system to segregate a wide range of protein complexes needed in the correct ratio to function properly. As this is a common system across bacteria, it could be harnessed to organise other protein complexes between bacteria. In many metabolic pathways efficient rates are achieved when proteins are closely associate ensuring local high concentrations and fast substrate transfer. If these pathways are expressed in alien systems the proteins are often diffuse and disorganised, resulting in inefficient rates of activity. In addition many proteins function with partner proteins and to understand how they work ideally their structures need to be characterised when bound, but usually the proteins are purified individually and mixed or when expressed individually they are insoluble. It is possible we can use this natural system for segregating protein complexes to keep other proteins in functional complexes and at high local concentrations. Using this reduced system we could either use the system in synthetic biology for allowing a daughter cells to segregate proteins in functional but high ratios for a pathway to efficiently produce a desired product or it will allow expression of protein partners in an environment that will allow their isolation and structural analysis. To be able to harness this newly identified mechanism we need to understand the essential components holding the proteins together as complexes, causing the protein complexes to duplicate and the association with the chromosome on the chromosome associated protein.
期刊论文(7)
专著(0)
科研奖励(0)
会议论文
DOI:
10.1093/femsre/fuy015
发表时间:
2018-06
期刊:
FEMS microbiology reviews
影响因子:
11.3
作者:
[Emilia M. F. Mauriello;Christopher W. Jones;A. Moine;J. Armitage]
通讯作者:
Emilia M. F. Mauriello;Christopher W. Jones;A. Moine;J. Armitage
DOI:
10.1038/s41598-017-04093-x
发表时间:
2017-07-04
期刊:
Scientific reports
影响因子:
4.6
作者:
[Folliard T, Mertins B, Steel H, Prescott TP, Newport T, Jones CW, Wadhams G, Bayer T, Armitage JP, Papachristodoulou A, Rothschild LJ]
通讯作者:
Rothschild LJ
Structure of bacterial cytoplasmic chemoreceptor arrays and implications for chemotactic signaling.
细菌细胞质化学感受器阵列的结构及其对趋化信号传导的影响。
DOI:
10.7554/elife.02151
发表时间:
2014-03-25
期刊:
eLife
影响因子:
7.7
作者:
[Briegel A, Ladinsky MS, Oikonomou C, Jones CW, Harris MJ, Fowler DJ, Chang YW, Thompson LK, Armitage JP, Jensen GJ]
通讯作者:
Jensen GJ
Understanding protein interaction and turnover in the bacterial flagellar motor
-
批准号:BB/M008657/1
-
项目类别:Research Grant
-
资助金额:$42.83万
-
财政年份:2015
-
负责人:Judith Armitage
-
依托单位:
Dynamics and Robustness in Biological Networks
-
批准号:BB/H531400/1
-
项目类别:Research Grant
-
资助金额:$4.3万
-
财政年份:2010
-
负责人:Judith Armitage
-
依托单位:
Chemosensory transduction and the cytoplasmic pathway of Rhodobacter sphaeroides
-
批准号:BB/F018630/1
-
项目类别:Research Grant
-
资助金额:$44.65万
-
财政年份:2008
-
负责人:Judith Armitage
-
依托单位:
Protein turnover studies using single-molecule microscopy in functional bacterial flagellar motors of live cells to assess molecular complex stability
-
批准号:BB/F021224/1
-
项目类别:Research Grant
-
资助金额:$101.45万
-
财政年份:2008
-
负责人:Judith Armitage
-
依托单位:
From Bacterial Chemotaxis to the Prediction of Complex Networks: The Oxford Integrative Systems Biology Centre
-
批准号:BB/D020190/1
-
项目类别:Research Grant
-
资助金额:$1138.29万
-
财政年份:2007
-
负责人:Judith Armitage
-
依托单位:
海外基金