RegulonDB RegulonDB 10.8: Gene Form
   

rpsM gene in Escherichia coli K-12 genome


Gene local context to scale (view description)

rpsK rpsM rpmJ DksA-ppGpp DksA-ppGpp Cis-reg anti-anti-terminator anti-terminator terminator TSS_3676 (cluster) TSS_3676 (cluster) TSS_3675 (cluster) TSS_3675 (cluster) TSS_3674 (cluster) TSS_3674 (cluster) rpsMp2 rpsMp2 TSS_3672 (cluster) TSS_3672 (cluster) TSS_3671 TSS_3671 TSS_3670 (cluster) TSS_3670 (cluster) TSS_3669 TSS_3669 rpsMp1 rpsMp1 TSS_3668 TSS_3668 TSS_3667 (cluster) TSS_3667 (cluster) TSS_3666 TSS_3666 TSS_3665 (cluster) TSS_3665 (cluster) TSS_3664 TSS_3664 TSS_3663 (cluster) TSS_3663 (cluster) TSS_3662 (cluster) TSS_3662 (cluster) TSS_3661 (cluster) TSS_3661 (cluster) TSS_3660 TSS_3660 TSS_3659 TSS_3659 TSS_3658 TSS_3658 TSS_3657 TSS_3657 TSS_3656 TSS_3656 TSS_3655 TSS_3655 TSS_3654 TSS_3654 TSS_3653 TSS_3653

Gene      
Name: rpsM    Texpresso search in the literature
Synonym(s): ECK3285, EG10912, b3298
Genome position(nucleotides): 3442115 <-- 3442471 Genome Browser
Strand: reverse
Sequence: Get nucleotide sequence FastaFormat
GC content %:  
51.82
External database links:  
ASAP:
ABE-0010809
CGSC:
219
ECHOBASE:
EB0905
OU-MICROARRAY:
b3298
PortEco:
rpsM
STRING:
511145.b3298
COLOMBOS: rpsM


Product      
Name: 30S ribosomal subunit protein S13
Synonym(s): RpsM
Sequence: Get amino acid sequence Fasta Format
Cellular location: ribosome,cytosol
Molecular weight: 13.099
Isoelectric point: 11.433
Motif(s):
 
Type Positions Sequence
83 -> 118 LGCYRGLRHRRGLPVRGQRTKTNARTRKGPRKPIKK
3 -> 108 RIAGINIPDHKHAVIALTSIYGVGKTRSKAILAAAGIAEDVKISELSEGQIDTLRDEVAKFVVEGDLRREISMSIKRLMDLGCYRGLRHRRGLPVRGQRTKTNART
114 -> 118 KPIKK
2 -> 118 ARIAGINIPDHKHAVIALTSIYGVGKTRSKAILAAAGIAEDVKISELSEGQIDTLRDEVAKFVVEGDLRREISMSIKRLMDLGCYRGLRHRRGLPVRGQRTKTNARTRKGPRKPIKK
89 -> 99 LRHRRGLPVRG

 

Classification:
Multifun Terms (GenProtEC)  
  2 - information transfer --> 2.3 - protein related --> 2.3.2 - translation
  2 - information transfer --> 2.3 - protein related --> 2.3.8 - ribosomal proteins
  6 - cell structure --> 6.6 - ribosomes
Gene Ontology Terms (GO)  
cellular_component GO:0005829 - cytosol
GO:0005840 - ribosome
GO:0015935 - small ribosomal subunit
GO:0022627 - cytosolic small ribosomal subunit
molecular_function GO:0003676 - nucleic acid binding
GO:0003735 - structural constituent of ribosome
GO:0005515 - protein binding
GO:0003723 - RNA binding
GO:0000049 - tRNA binding
GO:0019843 - rRNA binding
biological_process GO:0006412 - translation
Note(s): Note(s): ...[more].
Reference(s): [1] Abdurashidova GG., et al., 1985
[2] Abdurashidova GG., et al., 1985
[3] Abdurashidova GG., et al., 1985
[4] Babkina GT., et al., 1984
[5] Babkina GT., et al., 1984
[6] Babkina GT., et al., 1985
[7] Babkina GT., et al., 1986
[8] Bakardjieva A., et al., 1974
[9] Bausk EV., et al., 1985
[10] Bollen A., et al., 1975
[11] Brandt R., et al., 1992
[12] Brewer LA., et al., 1983
[13] Brimacombe R., et al., 1988
[14] Budker VG., et al., 1980
[15] Bunner AE., et al., 2010
[16] Capel MS., et al., 1988
[17] Dabbs ER. 1978
[18] Dzionara M., et al., 1977
[19] Ewald R., et al., 1976
[20] Gimautdinova OI., et al., 1981
[21] Gimautdinova OI., et al., 1981
[22] Gimautdinova OI., et al., 1982
[23] Gorelic L. 1976
[24] Graifer DM., et al., 1989
[25] Issinger OG., et al., 1975
[26] Iusupov MM., et al., 1986
[27] Jaskunas SR., et al., 1977
[28] Kaltschmidt E., et al., 1974
[29] Kastner B., et al., 1981
[30] Lake JA., et al., 1975
[31] Lambert JM., et al., 1983
[32] Lelong JC., et al., 1974
[33] Melancon P., et al., 1984
[34] Meng J., et al., 2012
[35] Mildenhall KB., et al., 2016
[36] Millon R., et al., 1980
[37] Montesano-Roditis L., et al., 1993
[38] Mueller F., et al., 1997
[39] Nowotny V., et al., 1988
[40] Olah TV., et al., 1993
[41] Olsson MO., et al., 1979
[42] Pintor-Toro JA., et al., 1979
[43] Rinke J., et al., 1976
[44] Samaha RR., et al., 1994
[45] Sarapuu T., et al., 1984
[46] Sarapuu T., et al., 1982
[47] Schendel PL., et al., 1976
[48] Singer P., et al., 1985
[49] Skold SE. 1981
[50] Sommer A., et al., 1974
[51] Spirin AS., et al., 1996
[52] Spitnik-Elson P., et al., 1982
[53] Stoffler-Meilicke M., et al., 1987
[54] Syu WJ., et al., 1989
[55] Syu WJ., et al., 1992
[56] Syu WJ., et al., 1989
[57] Tischendorf GW., et al., 1974
[58] Tukalo MA., et al., 1987
[59] Ulmer E., et al., 1978
[60] Walles-Granberg A., et al., 2001
[61] Wower J., et al., 1990
[62] Yusupov MM., et al., 1986
[63] Zimmermann RA., et al., 1972
External database links:  
DIP:
DIP-35855N
ECOCYC:
EG10912-MONOMER
ECOLIWIKI:
b3298
INTERPRO:
IPR001892
INTERPRO:
IPR027437
INTERPRO:
IPR010979
INTERPRO:
IPR018269
INTERPRO:
IPR019980
MINT:
MINT-1290225
PANTHER:
PTHR10871:SF1
PDB:
1M5G
PDB:
2YKR
PDB:
3J9Y
PDB:
3J9Z
PDB:
3JA1
PDB:
3JBU
PDB:
3JBV
PDB:
3JCD
PDB:
3JCE
PDB:
3JCJ
PDB:
3JCN
PDB:
4A2I
PDB:
4ADV
PDB:
4U1U
PDB:
4U1V
PDB:
4U20
PDB:
4U24
PDB:
4U25
PDB:
4U26
PDB:
4U27
PDB:
4V47
PDB:
4V48
PDB:
4V4H
PDB:
4V4Q
PDB:
4V4V
PDB:
4V4W
PDB:
4V50
PDB:
4V52
PDB:
4V53
PDB:
4V54
PDB:
4V55
PDB:
4V56
PDB:
4V57
PDB:
4V5B
PDB:
4V5H
PDB:
4V5Y
PDB:
4V64
PDB:
4V65
PDB:
4V66
PDB:
4V69
PDB:
4V6C
PDB:
4V6D
PDB:
4V6E
PDB:
4V6K
PDB:
4V6L
PDB:
4V6N
PDB:
4V6O
PDB:
4V6P
PDB:
4V6Q
PDB:
4V6R
PDB:
4V6S
PDB:
4V6T
PDB:
4V6V
PDB:
4V6Y
PDB:
4V6Z
PDB:
4V70
PDB:
4V71
PDB:
4V72
PDB:
4V73
PDB:
4V74
PDB:
4V75
PDB:
4V76
PDB:
4V77
PDB:
4V78
PDB:
4V79
PDB:
4V7A
PDB:
4V7B
PDB:
4V7C
PDB:
4V7D
PDB:
4V7I
PDB:
4V7S
PDB:
4V7T
PDB:
4V7U
PDB:
4V7V
PDB:
4V85
PDB:
4V89
PDB:
4V9C
PDB:
4V9D
PDB:
4V9O
PDB:
4V9P
PDB:
4WF1
PDB:
4WOI
PDB:
4WWW
PDB:
4YBB
PDB:
5AFI
PDB:
5H5U
PDB:
5IQR
PDB:
5IT8
PDB:
5J5B
PDB:
5J7L
PDB:
5J88
PDB:
5J8A
PDB:
5J91
PDB:
5JC9
PDB:
5JTE
PDB:
5JU8
PDB:
5KCR
PDB:
5KCS
PDB:
5KPS
PDB:
5KPV
PDB:
5KPW
PDB:
5KPX
PDB:
5L3P
PDB:
5LZA
PDB:
5LZB
PDB:
5LZC
PDB:
5LZD
PDB:
5LZE
PDB:
5LZF
PDB:
5MDV
PDB:
5MDW
PDB:
5MDY
PDB:
5MDZ
PDB:
5ME0
PDB:
5ME1
PDB:
5MGP
PDB:
5MY1
PDB:
5NO2
PDB:
5NO3
PDB:
5NO4
PDB:
5NP6
PDB:
5NWY
PDB:
5O2R
PDB:
5U4I
PDB:
5U9F
PDB:
5U9G
PDB:
5UYK
PDB:
5UYL
PDB:
5UYM
PDB:
5UYN
PDB:
5UYP
PDB:
5UYQ
PDB:
5UZ4
PDB:
5WDT
PDB:
5WE4
PDB:
5WE6
PDB:
5WFK
PDB:
6BU8
PDB:
6BY1
PDB:
6C4I
PDB:
6DNC
PDB:
6ENF
PDB:
6ENJ
PDB:
6ENU
PDB:
6GWT
PDB:
6GXM
PDB:
6GXN
PDB:
6GXO
PDB:
6GXP
PDB:
6H4N
PDB:
6H58
PDB:
6HRM
PDB:
6I7V
PDB:
6OFX
PDB:
6OG7
PDB:
6Q98
PDB:
6Q9A
PFAM:
PF00416
PRIDE:
P0A7S9
PRODB:
PRO_000023866
PROSITE:
PS00646
PROSITE:
PS50159
REFSEQ:
NP_417757
SMR:
P0A7S9
UNIPROT:
P0A7S9


Operon      
Name: rpsMKD-rpoA-rplQ         
Operon arrangement:
Transcription unit        Promoter
rpsMKD-rpoA-rplQ
rpsMKD-rpoA-rplQ


RNA cis-regulatory element    
Attenuation: Transcriptional
   
Cis-reg Alpha operon ribosome binding site
   
   


Elements in the selected gene context region unrelated to any object in RegulonDB      

  Type Name Post Left Post Right Strand Notes Evidence (Confirmed, Strong, Weak) References
  promoter TSS_3653 3441735 reverse nd [RS-EPT-CBR] [64]
  promoter TSS_3654 3441857 reverse nd [RS-EPT-CBR] [64]
  promoter TSS_3655 3441871 reverse nd [RS-EPT-CBR] [64]
  promoter TSS_3656 3441875 reverse nd [RS-EPT-CBR] [64]
  promoter TSS_3657 3441883 reverse nd [RS-EPT-CBR] [64]
  promoter TSS_3658 3442063 reverse nd [RS-EPT-CBR] [64]
  promoter TSS_3659 3442068 reverse nd [RS-EPT-CBR] [64]
  promoter TSS_3660 3442101 reverse nd [RS-EPT-CBR] [64]
  promoter TSS_3661 (cluster) 3442116 reverse For this promoter, there
Read more >
[RS-EPT-CBR] [64]
  promoter TSS_3662 (cluster) 3442120 reverse For this promoter, there
Read more >
[RS-EPT-CBR] [64]
  promoter TSS_3663 (cluster) 3442126 reverse For this promoter, there
Read more >
[RS-EPT-CBR] [64]
  promoter TSS_3664 3442245 reverse nd [RS-EPT-CBR] [64]
  promoter TSS_3665 (cluster) 3442346 reverse For this promoter, there
Read more >
[RS-EPT-CBR] [64]
  promoter TSS_3666 3442433 reverse nd [RS-EPT-CBR] [64]
  promoter TSS_3667 (cluster) 3442437 reverse For this promoter, there
Read more >
[RS-EPT-CBR] [64]
  promoter TSS_3668 3442439 reverse nd [RS-EPT-CBR] [64]
  promoter TSS_3669 3442518 reverse nd [RS-EPT-CBR] [64]
  promoter TSS_3670 (cluster) 3442552 reverse For this promoter, there
Read more >
[RS-EPT-CBR] [64]
  promoter TSS_3671 3442554 reverse nd [RS-EPT-CBR] [64]
  promoter TSS_3672 (cluster) 3442559 reverse For this promoter, there
Read more >
[RS-EPT-CBR] [64]
  promoter TSS_3674 (cluster) 3442593 reverse For this promoter, there
Read more >
[RS-EPT-CBR] [64]
  promoter TSS_3675 (cluster) 3442600 reverse For this promoter, there
Read more >
[RS-EPT-CBR] [64]
  promoter TSS_3676 (cluster) 3442604 reverse For this promoter, there
Read more >
[RS-EPT-CBR] [64]


Evidence    

 [RS-EPT-CBR] RNA-seq using two enrichment strategies for primary transcripts and consistent biological replicates



Reference(s)    

 [1] Abdurashidova GG., Nargizian MG., Rudenko NV., Turchinskii MF., Budovskii EI., 1985, [Contacts of ribosomal proteins with tRNAPhe and 16S RNA in analogs of the 30S initiation complex]., Mol Biol (Mosk) 19(2):553-7

 [2] Abdurashidova GG., Ovsepian VA., Budovskii EI., 1985, [Proteins contacting with peptidyl-tRNA at the A-site of the Escherichia coli ribosome after enzymatic and non-enzymatic binding of aminoacyl-tRNA]., Mol Biol (Mosk) 19(4):1148-52

 [3] Abdurashidova GG., Ovsepian VA., Chernyi AA., Kaminir LB., Budovskii EI., 1985, [Ribosomal proteins interacting with Phe-tRNAPhe during enzymatic binding with translating ribosome before and after the release of the elongation factor EF-Tu]., Mol Biol (Mosk) 19(3):800-4

 [4] Babkina GT., Bausk EV., Graifer DM., Karpova GG., Matasova NB., 1984, The effect of aminoacyl- or peptidyl-tRNA at the A-site on the arrangement of deacylated tRNA at the ribosomal P-site., FEBS Lett 170(2):290-4

 [5] Babkina GT., Bausk EV., Karpova GG., Matasova NB., Graifer DM., 1984, [Photoaffinity modification of Escherichia coli ribosomes near the tRNA-binding centers by tRNAPhe derivatives carrying arylazido groups on guanosine residues]., Mol Biol (Mosk) 18(5):1306-10

 [6] Babkina GT., Karpova GG., Matasova NB., Berzin' VM., Gren EIa., 1985, [Study of the mRNA-binding region of ribosomes at different steps of translation. II. Affinity modification of Escherichia coli ribosomes by benzylidene derivative of AUGU6 in the 70S initiation complex]., Mol Biol (Mosk) 19(4):1079-85

 [7] Babkina GT., Veniaminova AG., Vladimirov SN., Karpova GG., Yamkovoy VI., Berzin VA., Gren EJ., Cielens IE., 1986, Affinity labelling of Escherichia coli ribosomes with a benzylidene derivative of AUGU6 within initiation and pretranslocational complexes., FEBS Lett 202(2):340-4

 [8] Bakardjieva A., Crichton RR., 1974, Topography of Escherichia coli ribosomal proteins. The order of reactivity of thiol groups., Biochem J 143(3):599-606

 [9] Bausk EV., Graifer DM., Karpova GG., 1985, [Study of the photoaffinity modification of Escherichia coli ribosomes near the donor tRNA-binding center]., Mol Biol (Mosk) 19(2):545-52

 [10] Bollen A., Heimark RL., Cozzone A., Traut RR., Hershey JW., 1975, Cross-linking of initiation factor IF-2 to Escherichia coli 30 S ribosomal proteins with dimethylsuberimidate., J Biol Chem 250(11):4310-4

 [11] Brandt R., Gualerzi CO., 1992, Ribosomal localization of the mRNA in the 30S initiation complex as revealed by UV crosslinking., FEBS Lett 311(3):199-202

 [12] Brewer LA., Noller HF., 1983, Ribonucleic acid-protein cross-linking within the intact Escherichia coli ribosome, utilizing ethylene glycol bis[3-(2-ketobutyraldehyde) ether], a reversible, bifunctional reagent: identification of 30S proteins., Biochemistry 22(18):4310-5

 [13] Brimacombe R., Atmadja J., Stiege W., Schuler D., 1988, A detailed model of the three-dimensional structure of Escherichia coli 16 S ribosomal RNA in situ in the 30 S subunit., J Mol Biol 199(1):115-36

 [14] Budker VG., Kobets ND., Kollektsionok IE., Karpova GG., Grineva NI., 1980, [Affinity labeling of ribosomes from Escherichia coli with 4-(N-2-chloroethyl, N-methylamino)-benzaldehyde actyl derivatives of oligouridylates]., Mol Biol (Mosk) 14(3):507-16

 [15] Bunner AE., Nord S., Wikstrom PM., Williamson JR., 2010, The effect of ribosome assembly cofactors on in vitro 30S subunit reconstitution., J Mol Biol 398(1):1-7

 [16] Capel MS., Kjeldgaard M., Engelman DM., Moore PB., 1988, Positions of S2, S13, S16, S17, S19 and S21 in the 30 S ribosomal subunit of Escherichia coli., J Mol Biol 200(1):65-87

 [17] Dabbs ER., 1978, Kasugamycin-dependent mutants of Escherichia coli., J Bacteriol 136(3):994-1001

 [18] Dzionara M., Robinson SM., Wittmann-Liebold B., 1977, Secondary structures of proteins from the 30S subunit of the Escherichia coli ribosome., Hoppe Seylers Z Physiol Chem 358(8):1003-19

 [19] Ewald R., Pon C., Gualerzi C., 1976, Reactivity of ribosomal sulfhydryl groups in 30S ribosomal subunits of Escherichia coli and 30S-IF-3 complexes., Biochemistry 15(22):4786-91

 [20] Gimautdinova OI., Karpova GG., Knorre DG., Kobetz ND., 1981, The proteins of the messenger RNA binding site of Escherichia coli ribosomes., Nucleic Acids Res 9(14):3465-81

 [21] Gimautdinova OI., Karpova GG., Kobets ND., 1981, [Affinity labeling of the ribosomes from Escherichia coli by 4-(N-2-chloroethyl-N-methyl-aminobenzyl-5'-phosphoamide of heptauridylic acid]., Mol Biol (Mosk) 15(4):797-804

 [22] Gimautdinova OI., Karpova GG., Kozyreva NA., 1982, [Affinity labeling of ribosomes from Escherichia coli with 4-(N-2-chloroethyl-N-methylamino) benzyl-5'-phosphamides of oligouridylates of different length]., Mol Biol (Mosk) 16(4):752-62

 [23] Gorelic L., 1976, Photoinduced cross-linkage, in situ, of Escherichia coli 30S ribosomal proteins to 16S rRNA: identification of cross-linked proteins and relationships between reactivity and ribosome structure., Biochemistry 15(16):3579-90

 [24] Graifer DM., Babkina GT., Matasova NB., Vladimirov SN., Karpova GG., Vlassov VV., 1989, Structural arrangement of tRNA binding sites on Escherichia coli ribosomes, as revealed from data on affinity labelling with photoactivatable tRNA derivatives., Biochim Biophys Acta 1008(2):146-56

 [25] Issinger OG., Kiefer MC., Traut RR., 1975, Specificity of ATP-dependent and GTP-dependent protein kinases with respect to ribosomal proteins of Escherichia coli., Eur J Biochem 59(1):137-43

 [26] Iusupov MM., Spirin AS., 1986, [Study of the surface of Escherichia coli ribosomes and ribosomal particles by the tritium bombardment method]., Biokhimiia 51(11):1858-67

 [27] Jaskunas SR., Fallon AM., Nomura M., 1977, Identification and organization of ribosomal protein genes of Escherichia coli carried by lambdafus2 transducing phage., J Biol Chem 252(20):7323-36

 [28] Kaltschmidt E., Kahan L., Nomura M., 1974, In vitro synthesis of ribosomal proteins directed by Escherichia coli DNA., Proc Natl Acad Sci U S A 71(2):446-50

 [29] Kastner B., Stoffler-Meilicke M., Stoffler G., 1981, Arrangement of the subunits in the ribosome of Escherichia coli: demonstration by immunoelectron microscopy., Proc Natl Acad Sci U S A 78(11):6652-6

 [30] Lake JA., Kahan L., 1975, Ribosomal proteins S5, S11, S13 and S19 localized by electron microscopy of antibody-labeled subunits., J Mol Biol 99(4):631-44

 [31] Lambert JM., Boileau G., Cover JA., Traut RR., 1983, Cross-links between ribosomal proteins of 30S subunits in 70S tight couples and in 30S subunits., Biochemistry 22(16):3913-20

 [32] Lelong JC., Gros D., Gros F., Bollen A., Maschler R., Stoffler G., 1974, Function of individual 30S subunit proteins of Escherichia coli. Effect of specific immunoglobulin fragments (Fab) on activities of ribosomal decoding sites., Proc Natl Acad Sci U S A 71(2):248-52

 [33] Melancon P., Boileau G., Brakier-Gingras L., 1984, Cross-linking of streptomycin to the 30S subunit of Escherichia coli with phenyldiglyoxal., Biochemistry 23(26):6697-703

 [34] Meng J., Kanzaki G., Meas D., Lam CK., Crummer H., Tain J., Xu HH., 2012, A genome-wide inducible phenotypic screen identifies antisense RNA constructs silencing Escherichia coli essential genes., FEMS Microbiol Lett 329(1):45-53

 [35] Mildenhall KB., Wiese N., Chung D., Maples VF., Mohanty BK., Kushner SR., 2016, RNase E-based degradosome modulates polyadenylation of mRNAs after Rho-independent transcription terminators in Escherichia coli., Mol Microbiol 101(4):645-55

 [36] Millon R., Olomucki M., Le Gall JY., Golinska B., Ebel JP., Ehresmann B., 1980, Synthesis of a new reagent, ethyl 4-azidobenzoylaminoacetimidate, and its use for RNA-protein cross-linking within Escherichia coli ribosomal 30-S subunits., Eur J Biochem 110(2):485-92

 [37] Montesano-Roditis L., McWilliams R., Glitz DG., Olah TV., Perrault AR., Cooperman BS., 1993, Placement of dinitrophenyl-modified ribosomal proteins in totally reconstituted Escherichia coli 30 S subunits. Localization of proteins S6, S13, S16, and S18 by immune electron microscopy., J Biol Chem 268(25):18701-9

 [38] Mueller F., Brimacombe R., 1997, A new model for the three-dimensional folding of Escherichia coli 16 S ribosomal RNA. II. The RNA-protein interaction data., J Mol Biol 271(4):545-65

 [39] Nowotny V., Nierhaus KH., 1988, Assembly of the 30S subunit from Escherichia coli ribosomes occurs via two assembly domains which are initiated by S4 and S7., Biochemistry 27(18):7051-5

 [40] Olah TV., Perrault AR., Cooperman BS., Montesano-Roditis L., McWilliams R., Glitz DG., 1993, Incorporation of dinitrophenyl derivatives of proteins S6, S13, S16, and S18 into the 30 S subunit of Escherichia coli ribosomes by total reconstitution., J Biol Chem 268(25):18696-700

 [41] Olsson MO., Isaksson LA., 1979, Analysis of rpsD mutations in Escherichia coli. III. Effects of rpsD mutations on expression of some ribosomal protein genes., Mol Gen Genet 169(3):271-8

 [42] Pintor-Toro JA., Vazquez D., Palacian E., 1979, Reversible modification of Escherichia coli ribosomes with 2,3-dimethylmaleic anhydride. A new method to obtain protein-deficient ribosomal particles., Biochemistry 18(15):3219-23

 [43] Rinke J., Yuki A., Brimacombe R., 1976, Studies on the environment of protein S7 within the 30-S subunit Escherichia coli ribosomes., Eur J Biochem 64(1):77-89

 [44] Samaha RR., O'Brien B., O'Brien TW., Noller HF., 1994, Independent in vitro assembly of a ribonucleoprotein particle containing the 3' domain of 16S rRNA., Proc Natl Acad Sci U S A 91(17):7884-8

 [45] Sarapuu T., Ustav E., Villems R., 1984, The modelling of the decoding site of the Escherichia coli ribosome., Nucleic Acids Res 12(5):2499-508

 [46] Sarapuu T., Villems R., 1982, Polynucleotide . ribosomal-protein complexes and their decoding properties., Eur J Biochem 124(2):275-81

 [47] Schendel PL., Craven GR., 1976, Studies on the ability of partially iodinated 16S RNA to participate in 30S ribosome assembly., Nucleic Acids Res 3(11):3001-14

 [48] Singer P., Nomura M., 1985, Stability of ribosomal protein mRNA and translational feedback regulation in Escherichia coli., Mol Gen Genet 199(3):543-6

 [49] Skold SE., 1981, RNA-protein complexes identified by crosslinking of polysomes., Biochimie 63(1):53-60

 [50] Sommer A., Traut RR., 1974, Diagonal polyacrylamide-dodecyl sulfate gel electrophoresis for the identification of ribosomal proteins crosslinked with methyl-4-mercaptobutyrimidate., Proc Natl Acad Sci U S A 71(10):3946-50

 [51] Spirin AS., Agafonov DE., Kolb VA., Kommer A., 1996, [Topography of ribosomal proteins: reconsideration of of protein map of small ribosomal subunit]., Biokhimiia 61(11):1928-30

 [52] Spitnik-Elson P., Elson D., Avital S., Abramowitz R., 1982, A ribonucleoprotein fragment of the 30 S ribosome of E. coli: evidence for long range RNA-RNA interactions., Nucleic Acids Res 10(6):1995-2006

 [53] Stoffler-Meilicke M., Stoffler G., 1987, The topography of ribosomal proteins on the surface of the 30S subunit of Escherichia coli., Biochimie 69(10):1049-64

 [54] Syu WJ., Kahan B., Kahan L., 1989, Epitopes of Escherichia coli ribosomal protein S13., J Protein Chem 8(6):701-17

 [55] Syu WJ., Kahan L., 1992, Both ends of Escherichia coli ribosomal protein S13 are immunochemically accessible in situ., J Protein Chem 11(3):225-30

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RegulonDB