Three different prohormones yield a variety of Hydra-RFamide (Arg-Phe-NH2) neuropeptides in Hydra magnipapillata.

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Three different prohormones yield a variety of Hydra-RFamide (Arg-Phe-NH2) neuropeptides in Hydra magnipapillata. / Darmer, D; Hauser, F; Nothacker, H P; Bosch, T C; Williamson, M; Grimmelikhuijzen, C J.

In: Biochemical Journal, Vol. 332 ( Pt 2), 1998, p. 403-12.

Research output: Contribution to journalJournal articleResearchpeer-review

Harvard

Darmer, D, Hauser, F, Nothacker, HP, Bosch, TC, Williamson, M & Grimmelikhuijzen, CJ 1998, 'Three different prohormones yield a variety of Hydra-RFamide (Arg-Phe-NH2) neuropeptides in Hydra magnipapillata.', Biochemical Journal, vol. 332 ( Pt 2), pp. 403-12.

APA

Darmer, D., Hauser, F., Nothacker, H. P., Bosch, T. C., Williamson, M., & Grimmelikhuijzen, C. J. (1998). Three different prohormones yield a variety of Hydra-RFamide (Arg-Phe-NH2) neuropeptides in Hydra magnipapillata. Biochemical Journal, 332 ( Pt 2), 403-12.

Vancouver

Darmer D, Hauser F, Nothacker HP, Bosch TC, Williamson M, Grimmelikhuijzen CJ. Three different prohormones yield a variety of Hydra-RFamide (Arg-Phe-NH2) neuropeptides in Hydra magnipapillata. Biochemical Journal. 1998;332 ( Pt 2):403-12.

Author

Darmer, D ; Hauser, F ; Nothacker, H P ; Bosch, T C ; Williamson, M ; Grimmelikhuijzen, C J. / Three different prohormones yield a variety of Hydra-RFamide (Arg-Phe-NH2) neuropeptides in Hydra magnipapillata. In: Biochemical Journal. 1998 ; Vol. 332 ( Pt 2). pp. 403-12.

Bibtex

@article{3d42fec0ec2811dcbee902004c4f4f50,
title = "Three different prohormones yield a variety of Hydra-RFamide (Arg-Phe-NH2) neuropeptides in Hydra magnipapillata.",
abstract = "The freshwater polyp Hydra is the most frequently used model for the study of development in cnidarians. Recently we isolated four novel Arg-Phe-NH2 (RFamide) neuropeptides, the Hydra-RFamides I-IV, from Hydra magnipapillata. Here we describe the molecular cloning of three different preprohormones from H. magnipapillata, each of which gives rise to a variety of RFamide neuropeptides. Preprohormone A contains one copy of unprocessed Hydra-RFamide I (QWLGGRFG), II (QWFNGRFG), III/IV [(KP)HLRGRFG] and two putative neuropeptide sequences (QLMSGRFG and QLMRGRFG). Preprohormone B has the same general organization as preprohormone A, but instead of unprocessed Hydra-RFamide III/IV it contains a slightly different neuropeptide sequence [(KP)HYRGRFG]. Preprohormone C contains one copy of unprocessed Hydra-RFamide I and seven additional putative neuropeptide sequences (with the common N-terminal sequence QWF/LSGRFGL). The two Hydra-RFamide II copies (in preprohormones A and B) are preceded by Thr residues, and the single Hydra-RFamide III/IV copy (in preprohormone A) is preceded by an Asn residue, confirming that cnidarians use unconventional processing signals to generate neuropeptides from their precursor proteins. Southern blot analyses suggest that preprohormones A and B are each coded for by a single gene, whereas one or possibly two closely related genes code for preprohormone C. Northern blot analyses and in situ hybridizations show that the gene coding for preprohormone A is expressed in neurons of both the head and foot regions of Hydra, whereas the genes coding for preprohormones B and C are specifically expressed in neurons of different regions of the head. All of this shows that neuropeptide biosynthesis in the primitive metazoan Hydra is already rather complex. Udgivelsesdato: 1998-Jun-1",
author = "D Darmer and F Hauser and Nothacker, {H P} and Bosch, {T C} and M Williamson and Grimmelikhuijzen, {C J}",
note = "Keywords: Amino Acid Sequence; Animals; Base Sequence; Cloning, Molecular; Gene Expression; Hydra; In Situ Hybridization; Molecular Sequence Data; Neuropeptides; Protein Precursors; RNA, Antisense; RNA, Messenger; Sequence Analysis, DNA",
year = "1998",
language = "English",
volume = "332 ( Pt 2)",
pages = "403--12",
journal = "Biochemical Journal",
issn = "0264-6021",
publisher = "Portland Press Ltd.",

}

RIS

TY - JOUR

T1 - Three different prohormones yield a variety of Hydra-RFamide (Arg-Phe-NH2) neuropeptides in Hydra magnipapillata.

AU - Darmer, D

AU - Hauser, F

AU - Nothacker, H P

AU - Bosch, T C

AU - Williamson, M

AU - Grimmelikhuijzen, C J

N1 - Keywords: Amino Acid Sequence; Animals; Base Sequence; Cloning, Molecular; Gene Expression; Hydra; In Situ Hybridization; Molecular Sequence Data; Neuropeptides; Protein Precursors; RNA, Antisense; RNA, Messenger; Sequence Analysis, DNA

PY - 1998

Y1 - 1998

N2 - The freshwater polyp Hydra is the most frequently used model for the study of development in cnidarians. Recently we isolated four novel Arg-Phe-NH2 (RFamide) neuropeptides, the Hydra-RFamides I-IV, from Hydra magnipapillata. Here we describe the molecular cloning of three different preprohormones from H. magnipapillata, each of which gives rise to a variety of RFamide neuropeptides. Preprohormone A contains one copy of unprocessed Hydra-RFamide I (QWLGGRFG), II (QWFNGRFG), III/IV [(KP)HLRGRFG] and two putative neuropeptide sequences (QLMSGRFG and QLMRGRFG). Preprohormone B has the same general organization as preprohormone A, but instead of unprocessed Hydra-RFamide III/IV it contains a slightly different neuropeptide sequence [(KP)HYRGRFG]. Preprohormone C contains one copy of unprocessed Hydra-RFamide I and seven additional putative neuropeptide sequences (with the common N-terminal sequence QWF/LSGRFGL). The two Hydra-RFamide II copies (in preprohormones A and B) are preceded by Thr residues, and the single Hydra-RFamide III/IV copy (in preprohormone A) is preceded by an Asn residue, confirming that cnidarians use unconventional processing signals to generate neuropeptides from their precursor proteins. Southern blot analyses suggest that preprohormones A and B are each coded for by a single gene, whereas one or possibly two closely related genes code for preprohormone C. Northern blot analyses and in situ hybridizations show that the gene coding for preprohormone A is expressed in neurons of both the head and foot regions of Hydra, whereas the genes coding for preprohormones B and C are specifically expressed in neurons of different regions of the head. All of this shows that neuropeptide biosynthesis in the primitive metazoan Hydra is already rather complex. Udgivelsesdato: 1998-Jun-1

AB - The freshwater polyp Hydra is the most frequently used model for the study of development in cnidarians. Recently we isolated four novel Arg-Phe-NH2 (RFamide) neuropeptides, the Hydra-RFamides I-IV, from Hydra magnipapillata. Here we describe the molecular cloning of three different preprohormones from H. magnipapillata, each of which gives rise to a variety of RFamide neuropeptides. Preprohormone A contains one copy of unprocessed Hydra-RFamide I (QWLGGRFG), II (QWFNGRFG), III/IV [(KP)HLRGRFG] and two putative neuropeptide sequences (QLMSGRFG and QLMRGRFG). Preprohormone B has the same general organization as preprohormone A, but instead of unprocessed Hydra-RFamide III/IV it contains a slightly different neuropeptide sequence [(KP)HYRGRFG]. Preprohormone C contains one copy of unprocessed Hydra-RFamide I and seven additional putative neuropeptide sequences (with the common N-terminal sequence QWF/LSGRFGL). The two Hydra-RFamide II copies (in preprohormones A and B) are preceded by Thr residues, and the single Hydra-RFamide III/IV copy (in preprohormone A) is preceded by an Asn residue, confirming that cnidarians use unconventional processing signals to generate neuropeptides from their precursor proteins. Southern blot analyses suggest that preprohormones A and B are each coded for by a single gene, whereas one or possibly two closely related genes code for preprohormone C. Northern blot analyses and in situ hybridizations show that the gene coding for preprohormone A is expressed in neurons of both the head and foot regions of Hydra, whereas the genes coding for preprohormones B and C are specifically expressed in neurons of different regions of the head. All of this shows that neuropeptide biosynthesis in the primitive metazoan Hydra is already rather complex. Udgivelsesdato: 1998-Jun-1

M3 - Journal article

C2 - 9601069

VL - 332 ( Pt 2)

SP - 403

EP - 412

JO - Biochemical Journal

JF - Biochemical Journal

SN - 0264-6021

ER -

ID: 3046067