武昌六前鞭虫胞器超微结构的研究

对武昌六前鞭虫胞器的超微结构进行了观察,发现R鞭毛复合体的内下方有分散的微管,两根R鞭毛复合体之间和外方具少量的粗面内质网,而虫体周边分布较多.粗面内质同外周被发达的微管.生毛体与胞核之间有胞咽和小盾结构.胞质中有较多的食物泡,未见到线粒体、高尔基体和表膜下微管结构.另外对粗面内质网的结构、功能以及种的鉴定等方面也作了讨论.       

食物在贻贝棘尾虫(原生动物,纤毛虫)细胞内的消化过程

利用免疫荧光显微术、透射电镜及电镜酶细胞化学技术对食物在腹毛类纤毛虫-- 贻贝棘尾虫细胞内的消化过程进行了追踪观察.食物在进入消化腔隙的初期,外面包被着一层膜结构,但此外层膜很快被消化而消失;尔后食物在贻贝棘尾虫体内的消化过程可分为两种方式:一种方式为直接在消化腔隙内完成,此过程同1982年Kaul et al.和Das s et al.的报道;而另一部分食物的消化过程表现为食物逐步向细胞质内突入,以致最终完全被细胞质包围形成一被膜包裹的圆泡状结构;在此过程中,细胞质边缘突出众多含有酸性磷酸酶等物质的小囊泡结构,小囊泡与食物融合,其内的酸性磷酸酶等水解酶释放出来, 食物的表膜逐渐瓦解,个体逐渐变小,最终消化后的营养物质被释放到细胞的消化腔隙内; 这种食物通过胞口与胞咽达消化腔隙后,再由细胞质将其包裹形成的食物泡,我们称之为" 后成食物泡".这两种消化方式与贻贝棘尾虫的消化胞器为一腔隙结构相适应[动物学报 5 4(3):510-516,2008].     

纤毛虫念珠异列虫射出胞器的超微结构观察

应用扫描电镜术和透射电镜术显示,纤毛虫念珠异列虫(Anteholosticha monilata)的射出胞器早期发生在细胞质深处,附近有不同类型的囊泡结构。成熟后射出胞器向表膜迁移,结构由不同电子密度片层的体部、结晶状的中心轴杆部和多层膜的帽部组成。受外界刺激时胞器冲破皮层射出,形态呈"蘑菇"状。据上述观察结果推测:该射出胞器具有防御作用,它可能起源于高尔基体活动产生的小泡;在亲缘关系较近的纤毛虫中,其射出胞器可能具有相似的分化特征。     

草丛土毛虫皮层纤毛器的微管胞器研究

本文应用FLUTAX直接荧光标记和抗α-微管蛋白抗体免疫荧光标记．显示了土壤纤毛虫草丛土毛虫（Territricha stramenticola）的皮层纤毛器微管胞器．其中纤毛器基部微管按口围带、波动膜、额腹横棘毛、左右缘棘毛、背触毛等纤毛器图式分布和定位,口围带和波动膜基部含小膜微管托架、小膜附属微管和波动膜微管骨架网;额腹横棘毛基部含前纵微管束、后纵微管束和横微管束：左、右缘棘毛基部含前纵微管束、后纵微管束、横微管束及后微管芽;背触毛基部含前纵微管束、后纵微管柬。横棘毛基部含有较发达的横微管束,缘棘毛基部含后微管芽及其横微管束的定位可能具有本种纤毛虫细胞的特异性。纤毛器微管胞器在细胞表膜下分化形成的基部微管及其微管层使细胞的运动纤毛器与强固的微管骨架结构网相联系．其微管胞器的建构可能是细胞对土壤生存环境的一种适应．是细胞运动胞器的功能活动与环境相互作用的结果。形态发生中,老口围带微管是逐步进行更新的：老棘毛微管胞器对新结构的发生和形成具有定位和物质贡献的作用．并且老结构在新结构分化和成熟期间也经历了行使相应的生理功能及逐渐退化和失去功能的过程．     

魏氏拟尾柱虫腹皮层纤毛器微管胞器的形态及形态发生

应用荧光紫杉醇直接荧光标记和抗α-微管蛋白抗体免疫荧光标记显示,魏氏拟尾柱虫(Paraurostyla weissei)腹面皮层纤毛器微管胞器由口围带、波动膜、额腹横棘毛和左右缘棘毛等纤毛器微管、纤毛器基部附属微管等组成。其中口围带基部微管包括小膜托架、小膜附属微管;额腹横棘毛和左右缘棘毛基部附属微管包括前纵微管束、后纵微管束和横微管束,它们由各自的纤毛器基部向皮层细胞质不同方向发射,形成腹皮层表面下微管网。结果表明,魏氏拟尾柱虫的纤毛器骨架、纤毛器附属结构也是一类以微管蛋白为基本成分的微管胞器,其中缘棘毛基部附属微管具有不同于其他纤毛虫(例如棘尾虫)中所观察到的同种微管胞器的建构特征。形态发生中,前仔虫口围带在老结构位置形成,其结构建成与部分老口围带的更新有关;老缘棘毛的结构物质对新的左、右缘棘毛的发生可能具有定位作用及物质贡献,但此后新的左、右缘棘毛列分别在老缘棘毛的右侧形成,而并非是在老缘棘毛位置分化的。在有些细胞中,新的左缘棘毛左侧另有一列棘毛,这可能是形态发生中老的左缘棘毛退化不完全产生的。     

魏氏拟尾柱虫休眠包囊及其细胞器超微结构的观察

为研究纤毛虫休眠状态下细胞的分化及其胞器的特征,本文以透射电镜术显示,魏氏拟尾柱虫（Ｐａｒａｕｒｏｓｔｙｌａｗｅｉｓｓｅｉ）休眠包囊中,颗粒层壁内有小泡,表膜位置偶见小泡样结构,大部分线粒体以多个相互聚集在一起,自噬泡将线粒体等胞器包裹在内经历消化过程,细胞内膜系统十分发达。作者推测,颗粒层及表厝小泡可能是休眠细胞经由表膜进行物质交换的结构,自噬泡消化现象可能是细胞中物质和能量来源的主要途径。     

新伪尾柱虫腹皮层纤毛器微管胞器的形态和形态发生

应用荧光紫杉醇直接荧光标记法显示,腹毛目纤毛虫新伪尾柱虫(Pseudourostyla nova)腹皮层纤毛器微管胞器由口围带、波动膜、额腹横棘毛和左右缘棘毛等纤毛器微管及纤毛器基部附属微管组成.口围带基部含小膜托架及与托架相联系的肋壁微管,其中领部小膜托架间由"Λ"形微管相联接;额腹横棘毛基部含前纵微管束、后纵微管束、横微管束和周围微管束,其微管在不同棘毛基部的发达程度不一;缘棘毛基部含前纵微管束、后纵微管束.同时,对新伪尾柱虫纤毛器微管胞器的形态发生和生理改组过程进行了详细的追踪研究,并对细胞皮层的额腹棘毛定位及组成特征进行了补充报道.此外,发现形态发生末期新纤毛器微管形成时,残存部分老额棘毛、横棘毛和缘棘毛,此后老结构逐渐被吸收.结果表明,新伪尾柱虫的纤毛器基部微管具有其种的特异性,新纤毛器微管分化过程中老结构可能具有定位和物质贡献作用.     

绿草履虫-小球藻共生系统中共生藻对宿主细胞超微结构的影响

应用透射电镜术显示了含小球藻绿草履虫和人工诱导获得的无小球藻绿草履虫细胞的超微结构特征,无小球藻绿草履虫细胞内有大量处于不同消化阶段的食物泡及膜性小泡,在细胞质内常见有线粒体聚集分布以及内质网分布其中,细胞大核内核仁数目增多,并聚集形成多个核仁区。含小球藻绿草履虫中细胞膜性结构较少见,细胞大核中核仁数目较少。结果表明,小球藻共生体可能影响了宿主草履虫细胞中所述细胞器的功能,数量和分布,并影响了核仁的功能,数量和分布。     

阔口尖毛虫皮层纤毛器微管在不同生理条件下的分化

应用激光扫描共聚焦显微术,显示腹毛类纤毛虫阔口尖毛虫(Oxytricha platystoma)无性生殖过程中,新的口围带、波动膜、额腹横棘毛、左右缘棘毛微管先后分化,老纤毛器微管去分化,细胞分裂产生各含一套纤毛器微管的前、后两仔虫;生理改组过程中,口围带、波动膜、额腹横棘毛、左右缘棘毛微管发生去分化和再分化,细胞皮层微管胞器更新形成含一套纤毛器微管的新细胞。结果表明阔口尖毛虫在无性生殖和生理改组这两种不同的生理条件下,其纤毛器微管结构的形成或更新可能具有相同的细胞调控机制,形态发生中老纤毛器结构可能对新结构的发生和发育具有诱导定位和物质贡献的作用。     

原生动物贻贝棘尾虫微管胞器的荧光标记与显示

采用FLUTAX直接荧光标记和抗α微管蛋白抗体的间接免疫荧光标记显示,原生动物贻贝棘尾虫(Stylonychia mytilus)细胞微管胞器由口围带、波动膜、额腹横棘毛、左右缘棘毛、背纤毛等纤毛器微管骨架、纤毛器基部附属微管和其他皮层微管骨架组成。纤毛器微管骨架和基部附属微管按皮层纤毛模式定位;皮层左、右侧微管带和领肋壁微管等其他皮层微管构成细胞特定位置的皮层微管骨架,并可能为具有背腹分化的腹毛目纤毛虫所特有,对维持细胞背腹面的形态、支持附近纤毛器(如左、右缘棘毛)的运动起作用。本文较完整地阐述了其细胞骨架的三维构形,对于深入了解纤毛虫细胞微管骨架的结构和分布特征,进一步揭示微管类胞器的功能是有意义的。     

Upward organelle motility

<正>Eukaryotic cells contain a collection of membrane-bounded organelles,in addition to the nucleus,supporting the large size and diverse activities of this type of cell.Evolving with these compartments are filaments and enzymes that convert chemical energy into work(so-called motor proteins),a network collectively termed the cytoskeleton.Whether it is a chloroplast moving to optimally intercept light or the     

Plant organelle positioning

Correct positioning and active movement of organelles within cells are essential for cellular homeostasis and adaptation to external stresses. Unlike animal and fungal systems, plant organelle positioning has not yet been revealed at the molecular level. The recent development of organelle-targeting green fluorescent protein (GFP) constructs and genetic analyses using Arabidopsis thaliana have shed new light on the field of plant organelle positioning, which has been found to be regulated by mechanisms that are similar to and/or distinct from those used by animals and fungi.     

Cartography of an organelle

Peptide counting in mass spectrometry allows researchers to draw a quantitative proteomic map of the ER and Golgi.     

The incredible shrinking organelle

The mitochondrion is probably the evolutionary remnant of a bacterial symbiont, yet contemporary mitochondria are nothing like contemporary bacteria. Evolutionary shrinkage of the mitochondrial genome is well documented, but what about wholesale shrinkage of the organelle itself?Considering its central role in energy metabolism in almost all eukaryotes, the mitochondrion is an amazingly plastic organelle, both evolutionarily and functionally. The few genes that the mitochondrial genome (mitochondrial DNA; mtDNA) encodes are clearly bacterial in origin—emanating from the α-proteobacterial lineage—supporting the widely held view that the mitochondrion is the evolutionary remnant of a bacterial symbiont (Gray et al, 2001). However, contemporary mitochondria are nothing like contemporary bacteria. For one thing, even the most gene-rich mtDNA encodes far less genetic information than the most gene-poor bacterial genome, and mitochondrial genomes are different from bacterial genomes in form, organization and mode of expression; these features vary tremendously among diverse eukaryotes. Mitochondrial genomes might be circular, linear or even highly fragmented, and they might contain highly fragmented and rearranged genes. Only within a poorly studied group of eukaryotic microbes—protists—known as jakobid flagellates does the mtDNA resemble a typical, albeit highly reduced, bacterial genome.In addition, the mitochondrial proteome is not only overwhelmingly (>90%) encoded in the nucleus, but only a small proportion (10–15%) is demonstrably α-proteobacterial in evolutionary affiliation. Thus, in the evolutionary transition from bacterial symbiont to integrated organelle, the mitochondrion has undergone an impressive degree of re-tailoring, shedding the bulk of its genetic information and taking on proteins of diverse evolutionary origins. Moreover, this re-tailoring is highly variable within different eukaryotic lineages, with an intriguing chunk of the mitochondrial proteome seeming to be organism-specific—lacking demonstrable sequence homologues other than in very close evolutionary relatives.Although the evolutionary shrinkage of the mitochondrial genome is well-documented, what is less widely appreciated is the wholesale shrinkage of the organelle itself in certain anaerobic eukaryotes. Taken to its extreme, such shrinkage involves complete loss of the mitochondrial genome, with a consequent reduction in the structural complexity and biochemical versatility of the organelle. This simplification might include elimination of the electron-transport chain (ETC) and thus lead to inability of the resulting mitochondrion-related organelle (MRO) to carry out a key function of aerobic mitochondria: ATP synthesis through coupled oxidative phosphorylation (for a full account, see Hjort et al, 2010).One such MRO, the hydrogenosome, is a hydrogen-producing organelle that was originally characterized in an anaerobic protist, Trichomonas vaginalis. The T. vaginalis hydrogenosome lacks mtDNA as well as components of the classic mitochondrial ETC, relying instead on substrate-level phosphorylation to generate ATP. Initially, the resemblance between the anaerobic biochemistry of the T. vaginalis MRO and that of anaerobic bacteria such as Clostridia raised the possibility that the hydrogenosome might have a different evolutionary origin than the classic aerobic mitochondrion. However, studies of hydrogenosomal proteins have demonstrated that the hydrogenosome is an evolutionarily derived (remnant) mitochondrion. Hydrogenosomes have been found in eukaryotes that are widely separated in phylogenetic trees, and in such trees, anaerobic, hydrogenosome-containing eukaryotes are often interspersed with close relatives that grow aerobically and contain conventional mitochondria. This punctate phylogenetic distribution suggests that the transition from mitochondrion to hydrogenosome has happened repeatedly and independently throughout eukaryotic evolution.The mitosome, an even more shrunken MRO that has not only dispensed entirely with a genome, but also has no ATP-generating capacity. This MRO was discovered in anaerobic eukaryotes that were initially thought to lack mitochondria entirely, the postulate being that they diverged away from the main line of eukaryotic evolution prior to the symbiosis that led to the mitochondrion. However, in all supposedly amitochondriate protists that have been examined, a candidate mitosome has been identified. As with hydrogenosomes, a punctate phylogenetic distribution of mitosomes is emerging.Recently, intermediate forms of ''shrinking organelle'' have been identified in the anaerobic protists Nyctotherus ovalis, Blastocystis sp. and Proteromonas lacertae (Hjort et al, 2010; Pérez-Brocal et al, 2010; de Graaf et al, 2011), relatives of brown algae and diatoms. In these cases, regions of the mtDNA that code for terminal portions of the ETC and for the mitochondrial ATP synthase have been discarded. The remaining DNA specifies genes for components of a mitochondrial translation system, as well as subunits of a proton-pumping complex I (NADH:ubiquinone oxidoreductase); a remarkable example—comparing the ciliate Nyctotherus with the stramenopiles Blastocystsis or Proteromonas—of convergent mtDNA evolution. These observations suggest that the transitional MROs of Nyctotherus, Blastocystis and Proteromonas retain a partial ETC, as well as the ability to synthesize protein, whereas other data (EST surveys) indicate that they are metabolically more complex than either hydrogenosomes or mitosomes. The discovery of these particular MROs is important because their existence argues that the transition from fully fledged aerobic mitochondrion to fully fledged anaerobic mitosome proceeds through, and might stop at, several intermediate stages: a realization that not only dramatically emphasizes the evolutionary and functional versatility of the mitochondrion, but also opens the possibility that we might yet uncover still other variations of this incredible shrinking organelle.     

Regulation of organelle acidity

Intracellular organelles have characteristic pH ranges that are set and maintained by a balance between ion pumps, leaks, and internal ionic equilibria. Previously, a thermodynamic study by Rybak et al. (Rybak, S., F. Lanni, and R. Murphy. 1997. Biophys. J. 73:674-687) identified the key elements involved in pH regulation; however, recent experiments show that cellular compartments are not in thermodynamic equilibrium. We present here a nonequilibrium model of lumenal acidification based on the interplay of ion pumps and channels, the physical properties of the lumenal matrix, and the organelle geometry. The model successfully predicts experimentally measured steady-state and transient pH values and membrane potentials. We conclude that morphological differences among organelles are insufficient to explain the wide range of pHs present in the cell. Using sensitivity analysis, we quantified the influence of pH regulatory elements on the dynamics of acidification. We found that V-ATPase proton pump and proton leak densities are the two parameters that most strongly influence resting pH. Additionally, we modeled the pH response of the Golgi complex to varying external solutions, and our findings suggest that the membrane is permeable to more than one dominant counter ion. From this data, we determined a Golgi complex proton permeability of 8.1 x 10(-6) cm/s. Furthermore, we analyzed the early-to-late transition in the endosomal pathway where Na,K-ATPases have been shown to limit acidification by an entire pH unit. Our model supports the role of the Na,K-ATPase in regulating endosomal pH by affecting the membrane potential. However, experimental data can only be reproduced by (1) positing the existence of a hypothetical voltage-gated chloride channel or (2) that newly formed vesicles have especially high potassium concentrations and small chloride conductance.     

The organelle of death

The mitochondrial FOF1-ATPase proton pump is required for function of the proapoptotic protein BAX in yeast and mammalian cells Matsuyama, S., Xu, Q., Velours, J. and Reed, J.C. Mol. Cell. 1, 327–336     

Evidence for organelle origin

A selection of evaluations from Faculty of 1000 covering the Methanococcus maripaludis genome; recombination in animal mitochondria; modulating cell cycle progression; gene silencing by microRNA directed methylation; yeast DNA breakage and repair.