In Prokaryotes

the level of PolyP drops drastically under phosphate starvation, and the subsequent addition of orthophosphate to the medium restores the initial phosphate level (Nesmeyanova et al, 1973, 1974a,b Nesmeyanova, 2000). Some genetic manipulations increased the ability of E. coli to accumulate PolyP (Kato et al, 1993a Ilardoyoct al, 1994 Ohtake et al., 1994 Sharfstein et al., 1996). High levels of accumulation were achieved 

In some culture conditions, extracellular PolyP was identified as a good source of phosphate (Curless et al, 1996). Using a typical medium in a high-cell-density fermentation of E. coli, 40 % higher cell density was obtained when using PolyP instead of Pi as a phosphate source (Curless et al, 1996). It is probable that the expression of specific porins allows PolyP transfer from the culture medium into the cells. The outer membrane porin PhoE of E. coli (Bauer et al, 1989) and the OprO porin of Pseudomonas aeruginosa (Siehnel et al, 1992 Hancock etal, 1992), induced by phosphate starvation, are examples of proteins which prefere PP and PolyP rather than P . 

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MacKinnon, R., et al. Structural conservation in prokaryotic and eukaryotic potassium channels. Science 280 106-109, 1998. 

FIGURE 11.24 The properties of mRNA molecules in prokaryotic versus eukaryotic cells during transcription and translation. 

Keto add-dependent enzymes are involved in numerous reactions and are found in prokaryotes as well as eukaryotes. Apart from scopolamine and clavulanic add biosynthesis, a-keto add-dependent enzymes are also found in the biosynthetic... 

Genome Management in Prokaryotes Genome Management in Eukaryotes... 

The Shine-Salgano interaction is a base pairing interaction that occurs during translation initiation in prokaryotes between the Shine-Dalgarno sequence on messenger RNA (mRNA) and the anti-Shine-Dalgamo... 

Still more confusion plagued early researches, when it was not realized that the biosynthetic routes to thiamine in prokaryotes and eukaryotes are quite different, a fact not expected at the outset. Thus, evidence collected from the study of yeast could not be transposed to bacteria, and vice-versa. For instance, formate is a most efficient precursor of one of the carbon atoms of the pyrimidine part of thiamine (pyramine), both in yeasts and enterobacteria, but incorporates at C-2 in bacteria and at C-4 in yeast. However, as is briefly covered in Section VIII, this dichotomy of pathways might have a deep significance in the perspective of biochemical evolution during primitive life on Earth. 

Because sugars are involved in most of the mechanisms established for the synthesis of these heterocycles, the development of carbohydrate chemistry has been most helpful in these researches—especially for the preparation of specifically labeled molecules. Conversely, the contribution of these efforts to carbohydrate chemistry and biochemistry has shown the involvement in biosynthesis of 1 -deoxy-D-f/rreo-pentulose—scarcely before recognized and considered a rare sugar—and of fully functionalized pentuloses of still unknown configuration (or their phosphates). Finally, evidence has been found in prokaryotes for a most extraordinary transformation of 5-amino-l-(P-D-ribofuranosyl)imidazole 5 -phos-phate into a pyrimidine. Surely, this transformation should be explained in terms... 

Microtubules are universally present in eukaryotes from protozoa to the cells of higher animals and plants (Porter, 1966 Hardham and Gunning, 1978 Lloyd, 1987), but they are absent in mammalian erythrocytes and in prokaryotes. Microtubules participate in a number of cellular functions including the maintenance of cell shape and polarity, mitosis, cytokinesis, the positioning of organelles, intracellular transport to specific domains, axoplasmic transport, and cell locomotion. The diversity of microtubule fimctions suggests that not all microtubules are identical and that different classes of microtubules are present in different cell types or are localized in distinct domains in the same cell type (Ginzburg et al., 1989). 

In terms of evolutionary biology, the complex mitotic process of higher animals and plants has evolved through a progression of steps from simple prokaryotic fission sequences. In prokaryotic cells, the two copies of replicated chromosomes become attached to specialized regions of the cell membrane and are separated by the slow intrusion of the membrane between them. In many primitive eukaryotes, the nuclear membrane participates in a similar process and remains intact the spindle microtubules are extranuclear but may indent the nuclear membrane to form parallel channels. In yeasts and diatoms, the nuclear membrane also remains intact, an intranuclear polar spindle forms and attaches at each pole to the nuclear envelope, and a single kinetochore microtubule moves each chromosome to a pole. In the cells of higher animals and plants, the mitotic spindle starts to form outside of the nucleus, the nuclear envelope breaks down, and the spindle microtubules are captured by chromosomes (Kubai, 1975 Heath, 1980 Alberts et al., 1989). 

In prokaryotes, each reaction of Figure 34-2 is catalyzed by a different polypeptide. By contrast, in eukaryotes, the enzymes are polypeptides with multiple catalytic activities whose adjacent catalytic sites facilitate channeling of intermediates between sites. Three distinct multifunctional enzymes catalyze reactions 3, 4, and 6, reactions 7 and 8, and reactions 10 and 11 of Figure 34-2. 

Although tRNAs are quite stable in prokaryotes, they are somewhat less stable in eukaryotes. The opposite is tme for mRNAs, which are quite unstable in prokaryotes but generally stable in eukaryotic organisms. 

So far as is possible, the discussion in this chapter and in Chapters 37, 38, and 39 will pertain to mammalian organisms, which are, of course, among the higher eukaryotes. At times it will be necessary to refer to observations in prokaryotic organisms such as bacteria and viruses, but in such cases the information will be of a kind that can be extrapolated to mammalian organisms. 

Figure 36-16. The discontinuous poiymerization of deoxyribonucleotides on the lagging strand formation of Okazaki fragments during iagging strand DNA synthesis is illustrated. Okazaki fragments are 100-250 nt iong in eukaryotes, 1000-2000 bp in prokaryotes.

Busby S, Ebright RH Promoter structure, promoter recognition, and transcription activation in prokaryotes. Cell 1994 79 ... 

Eukaryotic DNA that is in an active region of chromatin can be transcribed. As in prokaryotic cells, a... 

GENE REGULATION IN PROKARYOTES EUKARYOTES DIFFERS IN IMPORTANT RESPECTS... 

PelZ is a hydrophilic protein of 420 amino acids with a short hydrophobic sequence at its N-terminal end which has Ae characteristics of the signal sequences of exported proteins. The signal peptide may be 24 amino acids long, which would corroborate wiA the usual length encountered in prokaryotes. The molecular cloning of the pelZ gene in an expression vector pT7-6 allowed for the specific 35S-cysteine-methionine raAo-labelling of PelZ in E. coli K38. We could detect, in crude extracts, the presence of a precursor and a mature form of PelZ. After cell fractionation, Ae mature form of PelZ could be localized in Ae periplasm of E. coli. So PelZ appears to be a protein exported by Ae Sec-dependent system of translocation. 

The Enzymes II (E-IIs) of the phosphoenolpyruvate (P-enolpyruvate)-dependent phosphotransferase system (PTS) are carbohydrate transporters found only in prokaryotes. They not only transport hexoses and hexitols, but also pentitols and disaccharides. The PTS substrates are listed in Table I. The abbreviations used (as superscripts) throughout the text for these substrates are as follows Bgl, jS-gluco-side Cel, cellobiose Fru, fructose Glc, glucose Gut, glucitol Lac, lactose Man, mannose Mtl, mannitol Nag, iV-acetylglucosamine Scr, sucrose Sor, sorbose Xtl, xylitol. 

FIGURE 3.17 Cytochrome P450 systems in prokaryotes and eukaryotes. (From Neilson, A.H. and Allard, A.-S. Microbial metabolism of PAHs and heteroarenes, The Handbook of Environmental Chemistry, Vol. 3J, pp. 1-80, Springer, 1998. With permission.)... 

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