This review summarizes the main results obtained in the fields of general and molecular microbiology and microbial genetics at the Institute of Microbiology of the Academy of Sciences of the Czech Republic (AS CR) [formerly Czechoslovak Academy of Sciences (CAS)] over more than 50 years. Contribution of the founder of the Institute, academician Ivan Málek, to the introduction of these topics into the scientific program of the Institute of Microbiology and to further development of these studies is also included.

• MeSH
• akademie a ústavy dějiny   MeSH
• dějiny 20. století MeSH
• mikrobiální genetika dějiny   MeSH
• molekulární biologie dějiny   MeSH
• Check Tag
• dějiny 20. století MeSH
• Publikační typ
• časopisecké články MeSH
• historické články MeSH
• práce podpořená grantem MeSH
• přehledy MeSH
• Geografické názvy
• Česká republika MeSH

In vitro phosphorylation of EF-Tu was shown in cell-free extract from dormant spores of Streptomyces coelicolor by a protein kinase present in spores. EF-Tu phosphorylation was observed on both intrinsic S. coelicolor factor and externally added purified EF-Tu from S. aureofaciens, on two isoforms. Putative serine and threonine residues as potential phosphorylation targets were determined in primary sequence and demonstrated on 3D structure model of EF-Tu.

• MeSH
• 2D gelová elektroforéza MeSH
• elongační faktor Tu chemie   izolace a purifikace   metabolismus   MeSH
• fosforylace MeSH
• molekulární modely MeSH
• molekulární sekvence - údaje MeSH
• proteinkinasy metabolismus   MeSH
• sekvence aminokyselin MeSH
• sekvenční seřazení MeSH
• spory bakteriální enzymologie   metabolismus   MeSH
• Streptomyces aureofaciens metabolismus   MeSH
• Streptomyces coelicolor metabolismus   MeSH
• terciární struktura proteinů MeSH
• zobrazování trojrozměrné MeSH
• Publikační typ
• časopisecké články MeSH
• práce podpořená grantem MeSH
• Názvy látek
• elongační faktor Tu MeSH
• proteinkinasy MeSH

We cloned EF-Tu from Streptomyces aureofaciens on a pET plasmid and overproduced it using the T7 RNA polymerase system in Escherichia coli. Streptomyces EF-Tu represented more than 40% of the total cell protein and was stored mostly in inclusion bodies formed apically at both ends of E. coli cells. Analysis of the inclusion bodies by transmission and scanning electron microscopy did not reveal any internal or surface ultrastructures. We developed the method for purification of S. aureofaciens EF-Tu from isolated inclusion bodies based on the ability of the protein to aggregate spontaneously. EF-Tu present in inclusion bodies was not active in GDP binding. Purified protein showed a similar charge heterogeneity as EF-Tu isolated from the mycelium of S. aureofaciens and all of the isoforms reacted with EF-Tu antibodies. All isoforms also reacted with monoclonal antibodies against O-phosphoserine and O-phosphothreonine.

• MeSH
• 2D gelová elektroforéza MeSH
• bakteriální proteiny genetika   imunologie   izolace a purifikace   metabolismus   MeSH
• buněčná inkluze ultrastruktura   MeSH
• elektroforéza v polyakrylamidovém gelu MeSH
• elongační faktor Tu genetika   imunologie   izolace a purifikace   metabolismus   MeSH
• Escherichia coli genetika   metabolismus   MeSH
• exprese genu MeSH
• genetické vektory MeSH
• guanosindifosfát metabolismus   MeSH
• klonování DNA MeSH
• mikroskopie elektronová rastrovací MeSH
• monoklonální protilátky imunologie   MeSH
• plazmidy MeSH
• posttranslační úpravy proteinů * MeSH
• protein - isoformy imunologie   MeSH
• rekombinantní proteiny imunologie   izolace a purifikace   metabolismus   MeSH
• Streptomyces aureofaciens genetika   MeSH
• transmisní elektronová mikroskopie MeSH
• vazba proteinů MeSH
• Publikační typ
• časopisecké články MeSH
• práce podpořená grantem MeSH
• Názvy látek
• bakteriální proteiny MeSH
• elongační faktor Tu MeSH
• guanosindifosfát MeSH
• monoklonální protilátky MeSH
• protein - isoformy MeSH
• rekombinantní proteiny MeSH

Protein kinases can be classified into two main superfamilies on the basis of their sequence similarity and substrate specificity. The protein His kinase superfamily which autophosphorylate a His residue, and superfamily Ser/Thr and Tyr protein kinases, which phosphorylate Ser, Thr or Tyr residues. During the last years genes encoding Ser/Thr protein kinases have been identified in several microorganisms. Phosphorylation of proteins on Ser/Thr residues can be involved in many functions of prokaryotic cells including cell differentiation, signal transduction and protein biosynthesis. Phosphorylation of prokaryotic protein-synthesizing systems showed that the phosphorylation of initiation and elongation factors is subject to alteration during cell differentiation or bacteriophage infection. Protein kinase associated with ribosomes of streptomycetes phosphorylate the elongation factor Tu and 11 ribosomal proteins even in bacteriophage-uninfected cells. After phosphorylation of ribosomal proteins, ribosomes lose about 30% of their activity at the translation of poly(U).

• MeSH
• bakteriální proteiny metabolismus   MeSH
• elongační faktor Tu metabolismus   MeSH
• fosforylace MeSH
• molekulární sekvence - údaje MeSH
• proteinkinasy metabolismus   MeSH
• ribozomální proteiny metabolismus   MeSH
• ribozomy metabolismus   MeSH
• sekvence aminokyselin MeSH
• Streptomyces enzymologie   MeSH
• Publikační typ
• časopisecké články MeSH
• práce podpořená grantem MeSH
• přehledy MeSH
• Názvy látek
• bakteriální proteiny MeSH
• elongační faktor Tu MeSH
• proteinkinasy MeSH
• ribozomální proteiny MeSH

Prokaryotic cells contain proteins which form extended chains or multimers that oscillate between monomers and oligomers of varying length. Hydrolysis of nucleoside triphosphates combined with site-specific disposition of substrates and products to monomers and multimers is the driving force of dynamic instability of these molecules. Polymeric structures are connected in some manner to a variety of signaling systems that adhere to the polymeric matrix, including the GTP-binding protein(s), protein kinases and phosphatases, and other proteins or systems that communicate between the cytoplasmic membrane and the cytosol. Flexible organization allowing regulated dynamic movement is one of the key elements in all living cells. In eukaryotic cells actin and tubulin are the two main components of dynamically controlled spatial system. These proteins are noteworthy for their ability to polymerize, reversibly, into filaments or microtubules in association with hydrolysis of ATP or GTP, respectively. As such, they regulate most of the mechanics of cell movement including cell division, cell differentiation, phagocytosis and other dynamic phenomena. Recent evidence revealed that microbial cells create functional domains at specific sites of the cells and can form cytoplasmic tubules and fibers.

• MeSH
• Bacteria růst a vývoj   metabolismus   MeSH
• bakteriální proteiny metabolismus   MeSH
• cytoskeletální proteiny * MeSH
• fosforylace MeSH
• fyziologie bakterií * MeSH
• mikrotubuly metabolismus   MeSH
• pohyb MeSH
• polymery metabolismus   MeSH
• proteiny vázající GTP chemie   metabolismus   MeSH
• tubulin chemie   metabolismus   MeSH
• Publikační typ
• časopisecké články MeSH
• práce podpořená grantem MeSH
• přehledy MeSH
• Názvy látek
• bakteriální proteiny MeSH
• cytoskeletální proteiny * MeSH
• FtsZ protein, Bacteria MeSH Prohlížeč
• polymery MeSH
• proteiny vázající GTP MeSH
• tubulin MeSH