The potential mRNA target sites for the ribosomal protein L10 found in Streptomyces griseus and S. coelicolor give evidence for the autogenous regulation of expression of the rplJL genes
On the basis of structural similarity between the m- and rRNA binding sites which underlies the molecular mechanism of the autogenous control of expression of the rplJL genes, mediated in prokaryotic organisms by ribosomal protein L10, we attempted to find the potential mRNA target sites in S. grise...
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Paton, E.B. 2019-06-17T08:53:52Z 2019-06-17T08:53:52Z 1995 The potential mRNA target sites for the ribosomal protein L10 found in Streptomyces griseus and S. coelicolor give evidence for the autogenous regulation of expression of the rplJL genes / E.В. Paton // Биополимеры и клетка. — 1995. — Т. 11, № 1. — С. 40-44. — Бібліогр.: 17 назв. — англ. 0233-7657 DOI: http://dx.doi.org/10.7124/bc.0003D0 https://nasplib.isofts.kiev.ua/handle/123456789/155628 577.21 On the basis of structural similarity between the m- and rRNA binding sites which underlies the molecular mechanism of the autogenous control of expression of the rplJL genes, mediated in prokaryotic organisms by ribosomal protein L10, we attempted to find the potential mRNA target sites in S. griseus and S. coelicolor. The potential targets found in both species of Streptomyces are of highly conserved structure and contain elements similar with the L10 binding domain of the 23S RNA. Compared to the L10, mRNA targets of Enterobacteria, Thermotoga maritima and Synechocystis, the target sites of Streptomyces contain a larger number of conserved and specific structural elements, similar in both analyzed species. Comparison of the structural organization of the "Streptomyces" and "Enterobacterial" types of the L10 mRNA targets with the structure of the L10 binding domain in the 23S RNA reveals that the elements, conserved in all the mentioned targets, are located in the ssA and dsA regions. The structure of the potential L10 mRNA target sites, which mimic the rRNA target of the regulatory ribosomal protein L10, gives evidence for the autogenous L1-0mediated control of expression of the rplJL genes in Streptomyces. Описано структурові особливості виявленого у представників Streptomyces постійного сайта зв'язування рибосомного білка L10, який розміщується в лідерній послідовності, що передує генам rplJL. Консервативність структурової організації сайта у двох видів Streptomyces і значна подібність структури до 23S мРНК свідчать про аутогенну регуляцію генів rplJL стрептоміцетів рибосомним білком L10. Описаны структурные особенности обнаруженного у представителей Streptomyces (Streptomyces griseus и Streptomyces coelicolor) потенциального сайта связывания рибосомного белка L10. расположенного в лидерной последовательности, предшествующей генам rplJL. Консервативность структурной организации сайта у двух видов Streptonmyces и высокое подобие структуры с 23S мРНК свидетельствуют об аутогенной регуляции экспрессии генов rplJL стриптомицетов рибосомным белком L10. en Інститут молекулярної біології і генетики НАН України Биополимеры и клетка The potential mRNA target sites for the ribosomal protein L10 found in Streptomyces griseus and S. coelicolor give evidence for the autogenous regulation of expression of the rplJL genes Потенційні мРНКові сайти-мішені для рибосомного білка L10, які виявлено у Streptomyces griseus i S. coelicolor, вказують на аутогенный контроль експресії генів rplJL Потенциальные мРНКовые сайты-мишени для рибосомного белка, обнаруженные у Streptomyces griseus и S. coelicolor, указывают на аутогенный контроль экспрессии генов rplJL Article published earlier |
| institution |
Digital Library of Periodicals of National Academy of Sciences of Ukraine |
| collection |
DSpace DC |
| title |
The potential mRNA target sites for the ribosomal protein L10 found in Streptomyces griseus and S. coelicolor give evidence for the autogenous regulation of expression of the rplJL genes |
| spellingShingle |
The potential mRNA target sites for the ribosomal protein L10 found in Streptomyces griseus and S. coelicolor give evidence for the autogenous regulation of expression of the rplJL genes Paton, E.B. |
| title_short |
The potential mRNA target sites for the ribosomal protein L10 found in Streptomyces griseus and S. coelicolor give evidence for the autogenous regulation of expression of the rplJL genes |
| title_full |
The potential mRNA target sites for the ribosomal protein L10 found in Streptomyces griseus and S. coelicolor give evidence for the autogenous regulation of expression of the rplJL genes |
| title_fullStr |
The potential mRNA target sites for the ribosomal protein L10 found in Streptomyces griseus and S. coelicolor give evidence for the autogenous regulation of expression of the rplJL genes |
| title_full_unstemmed |
The potential mRNA target sites for the ribosomal protein L10 found in Streptomyces griseus and S. coelicolor give evidence for the autogenous regulation of expression of the rplJL genes |
| title_sort |
potential mrna target sites for the ribosomal protein l10 found in streptomyces griseus and s. coelicolor give evidence for the autogenous regulation of expression of the rpljl genes |
| author |
Paton, E.B. |
| author_facet |
Paton, E.B. |
| publishDate |
1995 |
| language |
English |
| container_title |
Биополимеры и клетка |
| publisher |
Інститут молекулярної біології і генетики НАН України |
| format |
Article |
| title_alt |
Потенційні мРНКові сайти-мішені для рибосомного білка L10, які виявлено у Streptomyces griseus i S. coelicolor, вказують на аутогенный контроль експресії генів rplJL Потенциальные мРНКовые сайты-мишени для рибосомного белка, обнаруженные у Streptomyces griseus и S. coelicolor, указывают на аутогенный контроль экспрессии генов rplJL |
| description |
On the basis of structural similarity between the m- and rRNA binding sites which underlies the molecular mechanism of the autogenous control of expression of the rplJL genes, mediated in prokaryotic organisms by ribosomal protein L10, we attempted to find the potential mRNA target sites in S. griseus and S. coelicolor. The potential targets found in both species of Streptomyces are of highly conserved structure and contain elements similar with the L10 binding domain of the 23S RNA. Compared to the L10, mRNA targets of Enterobacteria, Thermotoga maritima and Synechocystis, the target sites of Streptomyces contain a larger number of conserved and specific structural elements, similar in both analyzed species. Comparison of the structural organization of the "Streptomyces" and "Enterobacterial" types of the L10 mRNA targets with the structure of the L10 binding domain in the 23S RNA reveals that the elements, conserved in all the mentioned targets, are located in the ssA and dsA regions. The structure of the potential L10 mRNA target sites, which mimic the rRNA target of the regulatory ribosomal protein L10, gives evidence for the autogenous L1-0mediated control of expression of the rplJL genes in Streptomyces.
Описано структурові особливості виявленого у представників Streptomyces постійного сайта зв'язування рибосомного білка L10, який розміщується в лідерній послідовності, що передує генам rplJL. Консервативність структурової організації сайта у двох видів Streptomyces і значна подібність структури до 23S мРНК свідчать про аутогенну регуляцію генів rplJL стрептоміцетів рибосомним білком L10.
Описаны структурные особенности обнаруженного у представителей Streptomyces (Streptomyces griseus и Streptomyces coelicolor) потенциального сайта связывания рибосомного белка L10. расположенного в лидерной последовательности, предшествующей генам rplJL. Консервативность структурной организации сайта у двух видов Streptonmyces и высокое подобие структуры с 23S мРНК свидетельствуют об аутогенной регуляции экспрессии генов rplJL стриптомицетов рибосомным белком L10.
|
| issn |
0233-7657 |
| url |
https://nasplib.isofts.kiev.ua/handle/123456789/155628 |
| citation_txt |
The potential mRNA target sites for the ribosomal protein L10 found in Streptomyces griseus and S. coelicolor give evidence for the autogenous regulation of expression of the rplJL genes / E.В. Paton // Биополимеры и клетка. — 1995. — Т. 11, № 1. — С. 40-44. — Бібліогр.: 17 назв. — англ. |
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2025-11-25T21:04:12Z |
| last_indexed |
2025-11-25T21:04:12Z |
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| fulltext |
УДК 577.21
Eugenia В. Paton
THE POTENTIAL mRNA TARGET SITES
FOR THE RIBOSOMAL PROTEIN LIO FOUND
IN STREPTOMYCES GRISEUS AND S. COELICOLOR
GIVE EVIDENCE FOR THE AUTOGENOUS REGULATION
OF EXPRESSION OF THE rplJL GENES
On the basis of structural similarity between the m- and rRNA binding sites which under*
lies the molecular mechanism of the autogenous control of expression of the rplJL
genes, mediated in prokaryotic organisms by ribosomal protein LIO, we attempted to
find the potential mRNA target sites in S. griseus and S. coelicolor. The potential
targets found in both species of Streptomyces are of highly conserved structure and
contain elements similar with the LIO binding domain of the 23S RNA. Compared to
the LIO, mRNA targets of Enterobacteria, Thermotoga maritima and Synechocystis, the
target sites of Streptomyces contain a larger number of conserved and specific stru
ctural elements, similar in both analyzed species. Comparison of the structural organi
zation of the «Streptomyces» and «Enterobacterial» types of the LIO mRNA targets
with the structure of the LIO binding domain in the 23S RNA reveals that the elements,
conserved in all the mentioned targets, are located in the ssA and dsA regions. The
structure of the potential LIO mRNA target sites, which mimic the rRNA target of the
regulatory ribosomal protein LIO, gives evidence for the autogenous LlO-mediated
control of expression of the rplJL genes in Streptomyces.
The expression of genes in the majority of ribosomal protein operons in
prokaryotic organisms is regulated autogenously at the translational le
vel [1]. This mode control is achieved due to the possibility of the re
gulatory ribosomal proteins, encoded by the mRNA of the controlled ope
rons, to bind in a competitive manner the target sites in the m- and rRNA.
The structural organization of these sites is highly homologous. In case
of the rplJL operon, whose genes are regulated by r-protein LIO (or its
1 :4 complex with L12) [2] we observed the possibility for heterologous
translational feedback control in Enterobacteria [3, 4], provided by the
highly conserved structure of both, the regulatory LIO proteins [5] and
their mRNA target sites [6]. Of particular interest is the fact, that in
case of the LIO target sites, whose structure is proved for Enterobacteria
[6] and putative — for Synechocystis PCC 6803 [7] and Thermotoga ma
ritima ([8]; Paton and Zhyvoloup, unpublished data), the degree of ho
mology between the mRNA target sites is higher than between the res
pective rRNA targets. Moreover, additional structural similarity between
the m- and rRNA targets of the LIO protein is characteristic of Entero
bacteria, Synechocystis and Thermotoga. This makes it reasonable to as
sume that the L10-RNA interaction, which mediates the autogenous re
gulation of the rplJL genes expression is species- and organism-specific.
Existence of the «specifying» complementary structural elements, is to
be found in both, the regulatory proteins [9] and their mRNA binding
sites [6—8]. The latter might be of importance to provide the efficient
recognition and tight binding the LIO protein to the mRNA, which in the
case of the rRNA target would be achieved via the cooperative binding
of the neighbouring r-proteins. Comparison of the LIO binding regions
in the rplJ leaders of seven enterobacterial species [6] reveals that the
AA1571 — 1572 (ennumeration as in E. coli [10, 11]), whose interaction
with the LIO protein had been proven by chemical analysis [11], are con-
© Eugenia B. Paton, 1996
40 ISSN 0233-7657. БИОПОЛИМЕРЫ И КЛЕТКА. 1995. Т. 11. № I
served. The conservation of AA1571—1572 in the potential LIO mRNA
targets of Synechocystis and Thermotoga (see Fig.) allows an assump
tion that AA1571—1572 in all o<f these mRNA targets, are involved in
binding to a complementary conserved structural elements of the regu
latory protein LIO. It is notable that the structural homologs of AA1571 —
1572 in the 23S rRNA belong to binding domain of r-protein LI I [12].
We reasoned that in other prokaryotic organisms whose rplJL genes were
feedback-regulated by LIO, the regulatory ZJ#-mRNA interaction might
also involve additional structural elements, however, possibly different
from AA1571—1572. The present paper is devoted to the analysis of the
rpU leader region of 5. griseus and S. coelicolor, whose nucleotide sequ
ence was recently determined [13, 14]. The special attempt was made to
find the potential LIO binding sites and, if it were the case, to compare
their structural organization in the both species to the structure of the
so far determined mRNA targets of LIO. The following logic underlied
the search for the potential LIO mRNA target sites.
The mRNA target site of the regulatory protein LIO is to be homo
logous to the rRNA target in as much as to provide the competitive bin
ding of the LIO protein. In all the cases documented so far [2, 6—8, 11]
the mRNA target sites for the LIO protein are located in the untranslated
rpU leader region. In both species of Streptomyces, the untranslated lea
der precedes the start of the LIO cistron. We further analysed the struc
tural homology of the rpU leaders of Streptomyces with the LIO mRNA
target sites of Enterobacteria, Synechocystis PCC 6803 and Thermotoga
maritima, as well as with the LIO binding domain of the 23S RNA of
Streptomyces ambofaciens (see Fig., A). The alignment of the nucleoti
de sequences was made using the ALIGN program (PCGENE software
package). The secondary structure prediction was carried out using the
RNAFOLD program (PCGENE). Motives of primary structure identical
to the Synechocystis and the Enterobacterial consensus LIO mRNA tar
get sites were found in the rpU leaders of both species of Streptomyces.
Further on, the secondary structure of the potential mRNA LIO binding
sites was calculated (results shown in Figure).
One can notice the pronounced similarity of structure of both S. gri
seus and S. coelicolor putative LIO binding sites with the consensus LIO
binding domain of the 23S RNA [12]. The most striking similarity with
the 23.S RNA is accounted for by the common general organization, whe
re of particular interest is the presence in the mRNA targets of Strepto
myces of the two (dsB and dsD) double-stranded regions, rather than a
single (dsB) region, which is typical for all of the so far known LIO
mRNA binding sites. The structural organization of the potential LIO
binding sites is highly similar in 5. griseus and S. coelicolor. The single-
stranded region С (ssC) is different from the relevant region of the 23S
RNA, as a well as from the other prokaryotic mRNA targets. The latter
would contain the typical conserved UUAA motif (see Fig., B). It is no
teworthy that the dsC regions are conserved in both types of mRNA tar
gets «enterobacterial» and «Streptomyces» like. However identical within
the two types of targets are only the two pairs, G-C and C-G in the dsC
region. The highest degree of homology of the mRNA targets in S. grise
us and 5. coelicolor is found in the dsC, ssA and sdA regions (see Fig.,
B). The structure in dsC region is completely conserved, except the in
ternal loop, which in 5. griseus is formed of the U, U, while in S. coeli
color— of U, C. The bulged nucleotides are typical structural elements
for the protein-nucleic acid interaction. Therefore, we should not exclude
the possible species-specifying role of the loop in the dsC region. The
dsB, dsC and dsD regions in both pro- and eukaryotic 23S RNA belong
to the Lll binding domain [12], which is interchangable for E. coli and
yeasts [15]. As already noticed, the mRNA targets of Enterobacteria, Sy
nechocystis and Thermotoga, although lacking the dsD region, do conta
in the conserved UUAA motif in the dsC (Fig.). Therefore the structural
similarity to the Lll binding domain of the 23S RNA is present in both
ISSN Ю233-7657. БИОПОЛИМЕРЫ И КЛЕТКА.. 1995. Т. П. № 1 4 1
The secondary structure of the rRNA (A) and
mRNA (B) binding sites of the ribosomal pro
tein L10: A — rRNA target sites (/ — the con
sensus secondary structure of L10 binding re
gion of the 23S rRNA [12]. Capitals denote
nucleotides conserved amongst at least 30 of
31 aligned 23S RNA of eukaryotes, archaebac-
teria and eubacteria; R and Y — conservations
as purines or pyrimidines. Base-pairs proven
by coordinated base changes in all three king
doms are denoted by lines; 2 — the secondary
structure of the L10 binding domain of the
S. ambofaciens 23S RNA [17]);£ — mRNA tar
get sites of L10 (1 — the potential LIO target
sites of S. griseus and 2 — S. coelicolor, lower
case letters denote nucleotides conserved in
both species; 3 — secondary structure of the po
tential L10 target site of Thermotoga maritima
based on the nucleotide sequence [6] and
mRNA secondary structure computation; 4 —
the potential target of the Synechocysils PCC
6B03 [7]; 5 — secondary structure of the con
sensus enterobacterial mRNA target based on
comoarison of the nucleotide sequences [2, 4] and secondary structure prediction. Asterisks denote the variable nucleotides; 6 — secondary structure of the
L10 mRNA target, consensus for Entervbacteria, Th. maritima and Synechocystis. Asterisks denote the variable nucleotides. The conserved base pairs are
denoted by lines
types of the mRNA L10 targets («Enterobacterial» and «Streptomyces»),
In Streptomyces, however, this similarity is much higher due to the pre
sence of the dsD region and therefore makes it tempting to assume that
Lll protein, in addition to L10, might be involved in Streptomyces in the
control of expression of the, rplJL genes. The functional role of Lll here
might consist in co-regulation of expression of the rplA and the rplJL
genes.
The structural elements which comprise the most important simila
rity between the two types of mRNA targets, the «Enterobacterial» and
«Streptomyces» like, are to be found in regions ssA and dsA. The con
served elements in the ssA region are: the AGA motif on the left side
and the A, adjacent to the first C-G pair of the dsA region, on the right
side of region ssA. The C-G pair is the most essential conservation in
the dsA region. The formation — of this C-G pair provides the most com
plete structural similarity between the m- and rRNA targets of Ы0 [16].
This feature is exploited in the models of the conformational switches of
the rplJ leaders of E. coli [2] and the six other species of Enterobacterid
[6], as well as those of Thermotoga maritima and Synechocystis (Paton,
and Zhyvoloup, unpublished) to explain the molecular mechanism of the
L/C-mediated feedback regulation. The conservation of the C-G pair (dsA),
and the adjacent A (ssA) in the putative mRNA target sites of the L10
protein of Streptomyces proves the functional importance of these ele
ments for L10 binding. The identical elements of the mRNA and rRNA
targets (ssA region and the C-G pair of dsA) suggest a complementary
structural conservation in the regulatory protein. We reason that the;
-RNTLL- motif, which is the only one conserved among the 17 analyzed
L10 protein sequences, is complementary to the conserved structural ele
ments in dsA and ssA regions of the RNA target sites [9].
It may be noted in conclusion that the potential L10 mRNA target
sites found in the two species of Streptomyces, S. griseus and S. coelico-
lor, prove once again the principle of feedback regulation of r-protein
synthesis in prokaryotic organisms being based on the structural simi
larity of the m- and rRNA targets, competitive for binding of the regula
tory proteins. Similarly to other prokaryotes, the mRNA target of LW
is located in Streptomyces in the untranslated rplJ leader region more
than a 100 nucleotides upstream the L10 start codon and therefore points
to the important functional role of the rplJ leader. The conserved struc
ture of the found potential Ы0 mRNA target is an evidence of its func
tional role for the autogenous control of expression of the rplJL genes
in Streptomyces. The structural specificity of the L10 mRNA targets fo
und in Streptomyces might reflect the degree of phylogenetic remoteness.
Given the peculiarities of the structural organization of the L10 target,
as well as of the whole rplJ leader region (Paton and Zhyvoloup, in pre
paration), one might expect some other specific features pertinent to the
molecular mechanism of the L/0-mediated autogenous control of the rplJL
genes expression in Streptomyces.
6. Б. Патон
ПОТЕНЦІЙНІ мРНКові САЙТИ-МІШЕНІ ДЛЯ РИБОСОМНОГО БІЛКА L10,
ЯКІ ВИЯВЛЕНО У STREPTOMYCES GRISEUS I S. COELICOLOR,
ВКАЗУЮТЬ НА АУТОГЕННЫЙ КОНТРОЛЬ ЕКСПРЕСІЇ ГЕНІВ rplJL
Р е з ю м е
Описано структурові особливості виявленого у представників Streptomyces постійно
го сайта зв'язування рибосомного білка L10, який розміщується в лідерній послідов
ності, що передує генам грЦЬ. Консервативність структурової організації сайта у
двох видів Streptomyces і значна подібність структури до 23S мРНК свідчать про
аутогенну регуляцію генів rplJL стрептоміцетів рибосомним білком L10.
ISSN 0233-7657. БИОПОЛИМЕРЫ И КЛЕТКА. 1995. Т. 11. № 1 43
REFERENCES
1. Lindahl L., Zengel J. M. Diverse mechanisms for regulating ribosomal protein syn
thesis in Escherichia coli // Progr. Nucl. Acids Res. and Мої. Biol.—1993.—N 1.—
P. 3—57.
2. Christensen Т., Johnsen ЛІ, Fiil N. P., Friesen J. D. RNA secondary structure and
translational inhibition: analysis of the mutants in the rplJ leader // EMBO J.—
1984.—3, N 7.—P. 1609—1612.
3. Paton E. В., Woodmaska M. I., Kroupskaya I. V. et al. Evidence for the ability of
the L10 ribosomal proteins of Salmonella typhimurium and Kttebsielta pneumoniae
to regulate rpIJL genes expression in E. coli // FEBS Let.—1990.—265, N 1, 2.—
P. 129—132.
4. Zhyvoloup A. N., Paton E. B. The E. coli ribosomal protein L10 of E. coli is ca
pable to regulate expression of the rpIJL genes in Citrobacter freundii // Biopoly-
mers and Cell.—1993.—9, N 6.—P. 88—100.
5. Paton E. В., Zhyvoloup A. N., Woodmaska M. I., Kroupskaya I. V. Nucleotide se
quence of the rpIJL operon and the deduced primary structure of the encoded L10
and L7/L12, proteins of S. typhimurium compared to that of E. coli // Nucl. Acids
Res.— 1990.— 18.— P. 4620.
6. Zhyvoloup A. N., Kroupskaya I. V., Lyaskovsky Т. Л1, Paton E. B. Comparison of
nucleotide sequences of the rplJ leader in Enter ob act eria 11 Biopolymers and Cell.—
1994.-10, N 1.—P. 37—40.
7. Schmidt L, Bubenko M., Subramanian A. A novel operon organization involving
the genes for the chorismate synthase aromatic biosynthesis pathway and ribosomal
GTPase center proteins Lll, LI, L10, LI2: rplKJL in Cyanobacterium synechocystis
PCC 6803 // J. Biol. Chem.—1993.—268, N 36.— P. 27447—27457.
8. Liao D., Dennis P. P. The organization and expression of essential transcription
translation component genes in the extremely thermophilic eubacterium Thermotoga
maritima // Ibid.— 1992.— 267, N 32.—P. 22787—22797.
9. Tereschcenko F. M., Paton E. B. Identification of the conserved structural elements
in the ribosomal protein L10 which are essential for the autogenous regulation of
gene expression in the rpIJL operon of Enterobacteria // Biolopymers and Cell.—
1995.—11, N 1.—P. 00—00.
10. Post L. E.t Strycharz C. D., Nomura M. et al. Nucleotide sequence of the ribosomal
protein cluster adjacent to the gene for RNA polymerase subunit b in Escherichia
coli II Proc. Nat. Acad. Sci. USA,—1979.—76/N 4.—P. 1697—1701.
11. Climie S. C, Friesen J. D. In vivo and in vitro structural analysis of the rplJ mRNA
leader in Escherichia coli // J. Biol. Chem.—1988.—263, N 29.—P. 16166—16175.
12. Egebjerg J., Douthwaite S. R., Liljas A., Garrett R. A. Characterization of the bin
ding sites of protein Lll and the L10 (L12) pentameric complex in the GTPase
domain of 23S ribosomal RNA from Escherichia coli // J. Мої. Biol.—1990.—213,
N 1.—P. 275—289.
13. Kuester K., Kuberski S., Piepersberg W., Distler J. Cloning and nucleotide sequence
analysis of the nusg-rplK, rplA, rplJ, rplL gene cluster of S. griseus // EMBL acces
sion N X72787.
14. Blanco G., Rodicio R.} Puglia A. M. et al. Synthesis of ribosomal proteins during
growth of Streptomyces coelicolor // EMBL accession N L24552.
15. Thompson J., Musters W., Cundliffe E.f Dahlberg A. E. Replacement of the Lll
binding region within E. coli 23S ribosomal RNA with its homologuc from yeast:
in vivo and in vitro analysis of hybrid ribosomes altered in the GTPase centre //
EMBO J.— 1993.— 12, N 4.—P. 1499—1504.
16. Draper D. E. How do proteins recognise specific RNA sites? New clews from auto-
genously regulated ribosomal proteins // Trends in Biochem. Sci.— 1989.—14, N 8.—
P. 335—338.
17. Gutell R. R., Schnare M. N., Gray M. W. A compilation of large subunit (23S-like)
ribosomal RNA sequences presented in a secondary structure format // Nucl. Acids
Res.—1991.—18, Suppl.—P. 2319.
Inst. Cell. Biol, and Genet. Engineer. 15.09.94
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