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The nucleotide sequence of human transition protein 1 cDNA

Authors:
H Luerssen
H Luerssen
H Luerssen
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Sigrid Hoyer-Fender at Georg-August-Universität Göttingen
Sigrid Hoyer-Fender
Wolfgang Engel
Wolfgang Engel
Wolfgang Engel
  • This person is not on ResearchGate, or hasn't claimed this research yet.
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Volume
16
Number
15
1988
Nucleic
Acids
Research
The
nucleotide
sequence
of
human
transition
protein
1
cDNA
H.Luerssen,
S.Hoyer-Fender
and
Wolfgang
Engel
Institute
fiir
Humangenetik
der
Universitit
G6ttingen,
Gosslerstrasse
12d,
D3400
G6ttingen,
FRG
Submitted
July
6,
1988
Accession
no.
X07948
We
screened
a
human
testis
cDNA
library
with
an
oligonucleotide
of
81
mer
prepared
according
to
a
part
of
the
published
nucleotide
sequence
of
the
rat
transition
protein
TP
1(1).
We
hiave
isolated
a
cDNA
clone
with
the
length
of
441
bp
containing
the
coding
regioon
of
162
bp
for
huiman
transition
protein
1.
There
is
about
84%
homology
in
the
coding
region
of
the
sequence
compared
to
rat.
The
insert
contains
the
full
3
-noncoding
region
with
215
bp
and
the
polyadenylationi-signal
186
bp
after
the
coding
region.
The
5
-noncoding
region
has
a
length
of
58
bp.
The
human
cDNA-clone
encodes
a
polypeptide
of
54
amino
acids
of
which
7
are
different
to
that
of
rat.
These
aminio
acids
are
underlined.
Human
transition
protein
1
lacks
cysteine,
glutamine,
glutamic
acid,
isoleucine,
phenylalanine,
and
tryptophane.
5'
AGCAAGAGCCGATCTCCTCACAAGGGAGTCAAGAGAGGTGGCAGCAAAAGAAAATACC
-50
-40
-30
-20
-10
ATG
TCG
ACC
AGC
CGC
AAA
TTA
AAG
AGT
CAT
GGC
ATG
AGG
AGG
AGC
AAG
AGC
CGA
1
S
T
S
R
K
L
K
S
H
G
M
R
R
S
K
S
R
TCT
CCT
CAC
AAG
GGA
GTC
AAG
AGA
GGT
GGC
AGC
AAA
AGA
AAA
TAC
CGT
AAG
GGC
S
P
H
K
G
V
K
RGG
S
K
R
K
Y
R
K
G
AAC
CTG
AAA
AGT
AGG
AAA
CGG
GGC
GAT
GAC
GCC
AAT
CGC
AAT
TAC
CGC
TCC
CAC
N L
K
S
R
K
R
G
D
D
A
N
R
N
Y
R
S
H
TTG TGA
GCCCCCAGCGGCTCTGCCCTGGTGCGCTTCACACAGCACCAAGCAGCAACAAGAACAGCAGAA
L
168
190
210
230
GGGGAACTGCCAAGGAGACCTGATGTTAGATCAAAGCCAGAGAGGAGCCTATGGAATGTGGATCAAATGCC
250
270
290
AGTTGTGACGAAATGAGGAATGTATATGTTGGCTGTTTTTCCCCAACATCTCAATAAAACTTTGAAAGCAA
310
330
350
370
AAAAAAAAAA
3'
383
Acknowledgment
This
work
was
supported
by
Deutsche
Forschungsgemeinschaft
(
En
84/1
8-3)
References
1.
Mohammad
A.
Heidaran
and
Stephen
Kistler
(1987)
Gene
54,
281-284
©
I
R
L
Press
Limited,
Oxford,
England.
7723

Supplementary resource (1)

Human mRNA for transition protein 1 (TP1)
Nucleotide Sequence
June 1988
H. Luerssen
... Replacement of histones with protamines pass first through another type of nuclear proteins called transitional proteins (TPs). Despite the presence of at least four transition proteins, in man (Luerssen et al., 1988) transitional proteins 1 (TP1) and 2 (TP2) are the major ones. Transition proteins, TP1 and TP2 are unique to mammalian spermatogenesis and play an important role in the spermiogenesis process. ...
View
... Replacement of histones with protamines pass first through another type of nuclear proteins called transitional proteins (TPs). Despite the presence of at least four transition proteins, in man (Luerssen et al., 1988) transitional proteins 1 (TP1) and 2 (TP2) are the major ones. Transition proteins, TP1 and TP2 are unique to mammalian spermatogenesis and play an important role in the spermiogenesis process. ...
View
... Replacement of histones with protamines pass first through another type of nuclear proteins called transitional proteins (TPs). Despite the presence of at least four transition proteins, in man (Luerssen et al., 1988) transitional proteins 1 (TP1) and 2 (TP2) are the major ones. Transition proteins, TP1 and TP2 are unique to mammalian spermatogenesis and play an important role in the spermiogenesis process. ...
Protamines and Sperm DNA Integrity of Smokers and Non-Smokers: Protamine and Smoking
Book
Full-text available
  • Oct 2011
The book clarify the negative effect of smoking on sperm quality at molecular biological level
View
... In Dictyostelium discoideum, different actin genes coding for the same actin are expressed differentially (46). From the results of the Northern blot analysis with the 3'-UT testicular SMGA probe of RNAs from smooth-muscle tissues (Fig. 3 (8,50), and mouse, rat, and human transition proteins (5,19,22,23,26,31; P. C. Yelick, Y. K. Kwon, J. F. Flynn, K. C. Kleene, and N. B. Hecht, Mol. Reprod. ...
View
Binding of a Phosphoprotein to the 3' Untranslated Region of the Mouse Protamine 2 mRNA Temporally Represses its Translation
Article
  • Oct 1993
The synthesis of the protamines, the predominant nuclear proteins of mammalian spermatozoa, is regulated during germ cell development by mRNA storage for about 7 days in the cytoplasm of differentiating spermatids. Two highly conserved sequences, the Y and H elements present in the 3' untranslated regions (UTRs) of all known mammalian protamine mRNAs, form RNA-protein complexes and specifically bind a protein of 18 kDa. Here, we show that translation of fusion mRNAs was markedly repressed in reticulocyte lysates supplemented with a mouse testis extract enriched for the 18-kDa protein when the mRNAs contained the 3' UTR of mouse protamine 2 (mP2) or the Y and H elements of mP2. No significant decrease was seen when the fusion mRNAs contained the 3' UTR of human growth hormone. The 18-kDa protein is developmentally regulated in male germ cells, requires phosphorylation for RNA binding, and is found in the ribonucleoprotein particle fractions of a testicular postmitochondrial supernatant. We propose that a phosphorylated 18-kDa protein plays a primary role in repressing translation of mP2 mRNA by interaction with the highly conserved Y and H elements. At a later stage of male gamete differentiation, the 18-kDa protein no longer binds to the mRNA, likely as a result of dephosphorylation, enabling the protamine mRNA to be translated.
View
Identification and developmental expression of a smooth-muscle gamma-actin in postmeiotic male germ cells of mice
Article
  • May 1989
Mouse testis contains two size classes of actin mRNAs of 2.1 and 1.5 kilobases (kb). The 2.1-kb actin mRNA codes for cytoplasmic beta- and gamma-actin and is found throughout spermatogenesis, while the 1.5-kb actin mRNA is first detected in postmeiotic cells. Here we identify the testicular postmeiotic actin encoded by the 1.5-kb mRNA as a smooth-muscle gamma-actin (SMGA) and present its cDNA sequence. The amino acid sequence deduced from the postmeiotic actin cDNA sequence was nearly identical to that of a chicken gizzard SMGA, with one amino acid replacement at amino acid 359, where glutamine was substituted for proline. The nucleotide sequence of the untranslated region of the SMGA differed substantially from those of other isotypes of mammalian actins. By using the 3' untranslated region of the testicular SMGA, a highly specific probe was obtained. The 1.5-kb mRNA was detected in RNA from mouse aorta, small intestine, and uterus, but not in RNA isolated from mouse brain, heart, and spleen. Testicular SMGA mRNA was first detected and increased substantially in amount during spermiogenesis in the germ cells, in contrast to the decrease of the cytoplasmic beta- and gamma-actin mRNAs towards the end of spermatogenesis. Testicular SMGA mRNA was present in the polysome fractions, indicating that it was translated. These studies demonstrate the existence of an SMGA in male haploid germ cells. The implications of the existence of an SMGA in male germ cells are discussed.
View
View
Mammalian Protamines: Structure and Molecular Interactions
Chapter
  • Jan 1989
During spermiogenesis in most vertebrates, the structure of spermatid chromatin is completely reorganized and the DNA is repackaged by a small, arginine-rich protein called protamine. As a consequence of the interactions that occur between DNA and protamine in late-step spermatids [1], the phosphodiester backbone of DNA is neutralized and the fibers of double-helical DNA and protamine coalesce into a maximally condensed [2], biochemically inert state. The resulting DNA-protamine complex is insoluble, enzymatic processes such as DNA repair are inhibited [3,4], and the genome is rendered genetically inactive [5]. Although we have learned a great deal about the structure, metabolism, and potential function of the protamines in the past two decades, we have learned comparatively little about the actual molecular structure of the DNA-protamine complex. The marked insolubility of sperm chromatin and the high affinity of protamine for DNA have often made it difficult to characterize the structure of sperm chromatin using the biochemical and physical techniques that have been applied to somatic chromatin and other DNA-protein complexes.
View
The spermatid, an unrecognized germ cell
Article
  • Mar 1997
The use of microinsemination of round or elongated spermatids into ovocytes, in certain cases of male infertility, requires re-examination of the sequence of morphological and functional changes that occur throughout spermiogenesis. This paper reviews essential findings on morphogenesis of spermatids, genome expression during sperm differentiation and cellular interactions between spermatids themselves and between spermatids and Sertoli cells. Round and elongated spermatids appear to represent two classes of structurally and functionally different cells. One question remains: on what criteria can one claim that a round spermatid functions normally when spermiogenesis is blocked or impaired?.
View
Binding ofaPhosphoprotein tothe3'Untranslated Region of theMouseProtamine 2mRNA Temporally Represses ItsTranslation
Article
Thesynthesis oftheprotamines, thepredominant nuclear proteins ofmammalian spermatozoa, isregulated during germcell development bymRNA storage forabout7 daysinthecytoplasm ofdifferentiating spermatids. Twohighly conserved sequences, theY andH elements present inthe3'untranslated regions (UTRs) ofallknownmammalian protamine mRNAs,formRNA-protein complexes andspecifically binda protein of18kDa.Here, weshowthattranslation offusion mRNAswasmarkedly repressed inreticulocyte lysates supplemented withamousetestis extract enriched forthe18-kDa protein whenthemRNAscontained the3'UTRofmouseprotamine 2(mP2) ortheYandH elements ofmP2.Nosignificant decrease wasseenwhen thefusion mRNAscontained the3'UTRofhumangrowth hormone. The18-kDa protein isdevelopmentally regulated inmalegermcells, requires phosphorylation forRNAbinding, andisfound intheribonucleoprotein particle fractions ofatesticular postmitochondrial supernatant. We propose thataphosphorylated 18-kDa protein plays aprimary role inrepressing translation ofmP2mRNA byinteraction withthehighly conserved Y andH elements. Atalater stage ofmalegamete differentiation, the18-kDa protein nolonger binds tothe mRNA,likely asaresult ofdephosphorylation, enabling theprotamine mRNA tobetranslated. Manyeukaryotic mRNAs contain regulatory elements thatcontrol their posttranscriptional utilization. Thesereg- ulatory elements often reside within the5'and3'untrans- lated regions (UTRs) ofmRNAs andinteract withspecific cytoplasmic proteins that modulate stability ortranslational competence ofmRNAs.Oneofthebest-characterized sys-
View
Isolation of a cDNA clone for transition protein 1 (TP1), a major chromosomal protein of mammalian spermatids
Article
  • Feb 1987
  • GENE
We have isolated a cDNA clone for rat transition protein 1 (TP1), a major chromosomal protein of mammalian spermatids. The clone was identified initially by hybrid selection of TP1 mRNA. The sequence of the 251-nucleotide cDNA includes the entire coding region for the protein, thereby confirming the identity of the clone as well as predicting two changes in the published amino acid sequence.
View
  • Jan 1987
  • 281-284
  • A Mohammad
  • Stephen Heidaran
  • Kistler
Mohammad A. Heidaran and Stephen Kistler (1987) Gene 54, 281-284