50S ribosomal protein L12P; Reviewed

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gi 663524437   1 MEYVYAAMLLHSAENEINEKNVGAVLKAAGVSSDDARVKALVASLGDVDIGEAM 54
Cdd:PRK06402   1 MEYIYAALLLHSAGKEINEDNLKKVLEAAGVEVDEARVKALVAALEDVNIEEAI 54

50S ribosomal protein L12P; Reviewed

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                 ....*....|....*....|....*....|....*....|....*....|....
gi 663524437   1 MEYVYAAMLLHSAENEINEKNVGAVLKAAGVSSDDARVKALVASLGDVDIGEAM 54
Cdd:PRK06402   1 MEYIYAALLLHSAGKEINEDNLKKVLEAAGVEVDEARVKALVAALEDVNIEEAI 54

Ribosomal protein L12p. This subfamily includes archaeal L12p, the protein that is functionally equivalent to L7/L12 in bacteria and the P1 and P2 proteins in eukaryotes. L12p is homologous to P1 and P2 but is not homologous to bacterial L7/L12. It is located in the L12 stalk, with proteins L10, L11, and 23S rRNA. L12p is the only protein in the ribosome to occur as multimers, always appearing as sets of dimers. Recent data indicate that most archaeal species contain six copies of L12p (three homodimers), while eukaryotes have four copies (two heterodimers), and bacteria may have four or six copies (two or three homodimers), depending on the species. The organization of proteins within the stalk has been characterized primarily in bacteria, where L7/L12 forms either two or three homodimers and each homodimer binds to the extended C-terminal helix of L10. L7/L12 is attached to the ribosome through L10 and is the only ribosomal protein that does not directly interact with rRNA. Archaeal L12p is believed to function in a similar fashion. However, hybrid ribosomes containing the large subunit from E. coli with an archaeal stalk are able to bind archaeal and eukaryotic elongation factors but not bacterial elongation factors. In several mesophilic and thermophilic archaeal species, the binding of 23S rRNA to protein L11 and to the L10/L12p pentameric complex was found to be temperature-dependent and cooperative.

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                 ....*....|....*....|....*....|....*....|....*....|....
gi 663524437   1 MEYVYAAMLLHSAENEINEKNVGAVLKAAGVSSDDARVKALVASLGDVDIGEAM 54
Cdd:cd05832    1 MEYIYAALLLHYAGKEINEENLKKVLEAAGIEVDEARVKALVAALEEVNIDEAI 54

50S ribosomal protein L12P; Reviewed

                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....
gi 663524437   1 MEYVYAAMLLHSAENEINEKNVGAVLKAAGVSSDDARVKALVASLGDVDIGEAM 54
Cdd:PRK06402   1 MEYIYAALLLHSAGKEINEDNLKKVLEAAGVEVDEARVKALVAALEDVNIEEAI 54

Ribosomal protein L12p. This subfamily includes archaeal L12p, the protein that is functionally equivalent to L7/L12 in bacteria and the P1 and P2 proteins in eukaryotes. L12p is homologous to P1 and P2 but is not homologous to bacterial L7/L12. It is located in the L12 stalk, with proteins L10, L11, and 23S rRNA. L12p is the only protein in the ribosome to occur as multimers, always appearing as sets of dimers. Recent data indicate that most archaeal species contain six copies of L12p (three homodimers), while eukaryotes have four copies (two heterodimers), and bacteria may have four or six copies (two or three homodimers), depending on the species. The organization of proteins within the stalk has been characterized primarily in bacteria, where L7/L12 forms either two or three homodimers and each homodimer binds to the extended C-terminal helix of L10. L7/L12 is attached to the ribosome through L10 and is the only ribosomal protein that does not directly interact with rRNA. Archaeal L12p is believed to function in a similar fashion. However, hybrid ribosomes containing the large subunit from E. coli with an archaeal stalk are able to bind archaeal and eukaryotic elongation factors but not bacterial elongation factors. In several mesophilic and thermophilic archaeal species, the binding of 23S rRNA to protein L11 and to the L10/L12p pentameric complex was found to be temperature-dependent and cooperative.

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                 ....*....|....*....|....*....|....*....|....*....|....
gi 663524437   1 MEYVYAAMLLHSAENEINEKNVGAVLKAAGVSSDDARVKALVASLGDVDIGEAM 54
Cdd:cd05832    1 MEYIYAALLLHYAGKEINEENLKKVLEAAGIEVDEARVKALVAALEEVNIDEAI 54

Ribosomal protein P1, P2, and L12p. Ribosomal proteins P1 and P2 are the eukaryotic proteins that are functionally equivalent to bacterial L7/L12. L12p is the archaeal homolog. Unlike other ribosomal proteins, the archaeal L12p and eukaryotic P1 and P2 do not share sequence similarity with their bacterial counterparts. They are part of the ribosomal stalk (called the L7/L12 stalk in bacteria), along with 28S rRNA and the proteins L11 and P0 in eukaryotes (23S rRNA, L11, and L10e in archaea). In bacterial ribosomes, L7/L12 homodimers bind the extended C-terminal helix of L10 to anchor the L7/L12 molecules to the ribosome. Eukaryotic P1/P2 heterodimers and archaeal L12p homodimers are believed to bind the L10 equivalent proteins, eukaryotic P0 and archaeal L10e, in a similar fashion. P1 and P2 (L12p, L7/L12) are the only proteins in the ribosome to occur as multimers, always appearing as sets of dimers. Recent data indicate that most archaeal species contain six copies of L12p (three homodimers), while eukaryotes have two copies each of P1 and P2 (two heterodimers). Bacteria may have four or six copies (two or three homodimers), depending on the species. As in bacteria, the stalk is crucial for binding of initiation, elongation, and release factors in eukaryotes and archaea.

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gi 663524437   1 MEYVYAAMLLHSAENEINEKNVGAVLKAAGVSSDDARVKALVASLGDVDIGEAM 54
Cdd:cd04411    1 MEYVAAYLLLHKGGKELTEDKIKELLSAAGAEIEPERVKLFLSALNGKNIDEVI 54